|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
69-560 |
0e+00 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 829.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 69 KNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQAN 148
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 149 VSILIVENDQQLQKILLIPpDKMETVKAIVQYKLPLMESMANLYSWNDFMELGNDIPNIQLDRVILSQKANQCAVILYTS 228
Cdd:cd05933 81 ANILVVENQKQLQKILQIQ-DKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 229 GTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDALRGTLVYT 308
Cdd:cd05933 160 GTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 309 LQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRMLGKRDIPMNYRMAKALVFAKVRTSLGL 388
Cdd:cd05933 240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 389 DNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQNKEGVGEVCMWG 468
Cdd:cd05933 320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 469 RHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKEKIPIISHAMLVGD 548
Cdd:cd05933 400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGD 479
|
490
....*....|..
gi 569000640 549 KAKFLCMLLTLK 560
Cdd:cd05933 480 KRKFLSMLLTLK 491
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
44-559 |
9.64e-166 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 484.22 E-value: 9.64e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 44 ETPMTIPELFQESAERFSAYPALASKNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTIL 123
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 124 AGGLCVGIYATNSAEACQYVIQQANVSILIVENDQQLQKILLIpPDKMETVKAIVQYKLPLMESMANLYSWNDFMELGND 203
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV-RDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 204 IPN-IQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSHIAAQLTD 282
Cdd:COG1022 167 VADpAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPL----GPGDRTLSFLPLAHVFERTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 283 IWIpIKIGALTFFAQ-PDalrgTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRM 361
Cdd:COG1022 243 YYA-LAAGATVAFAEsPD----TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 362 LGKRdIP----MNYRMAKALVFAKVRTSLGlDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVY 437
Cdd:COG1022 318 AGKS-PSlllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 RVLSCGKVLSGCKnmlynqnkegV-----GEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRI 512
Cdd:COG1022 396 RIGTVGPPLPGVE----------VkiaedGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRK 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 569000640 513 KEILITAGGENVSPIPIETLVKEkIPIISHAMLVGDKAKFLCMLLTL 559
Cdd:COG1022 466 KDLIVTSGGKNVAPQPIENALKA-SPLIEQAVVVGDGRPFLAALIVP 511
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
74-559 |
2.00e-128 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 383.48 E-value: 2.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 74 WDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILI 153
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 154 VENdqqlqkillipPDkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkanQCAVILYTSGTTGT 233
Cdd:cd05907 83 VED-----------PD--------------------------------------------------DLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 234 PKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDAlrgTLVYTLQEVK 313
Cdd:cd05907 102 PKGVMLSHRNILSNALALAERLPA----TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 314 PTLFMGVPRIWEKMQDTIKenVARSSRLRKKAFAWAKmlglkvntkrmlgkrdipmnyrmakalvfakvrtslgLDNCHA 393
Cdd:cd05907 175 PTVFLAVPRVWEKVYAAIK--VKAVPGLKRKLFDLAV-------------------------------------GGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 394 FFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQnkegvGEVCMWGRHVFM 473
Cdd:cd05907 216 AASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPNVML 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 474 GYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKEKiPIISHAMLVGDKAKFL 553
Cdd:cd05907 291 GYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFL 369
|
....*.
gi 569000640 554 CMLLTL 559
Cdd:cd05907 370 VALIVP 375
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
53-519 |
6.24e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 285.75 E-value: 6.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 53 FQESAERFSAYPALaskNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIY 132
Cdd:pfam00501 1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 133 ATNSAEACQYVIQQANVSILIVENDQQLQKILLIPPDKMETVKAIVQYKLPLMEsmanlYSWNDFMELGNDIPNIQLDRV 212
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLK-----EEPLPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 213 ilsqKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGAL 292
Cdd:pfam00501 153 ----DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 293 TFFAQPDALR--GTLVYTLQEVKPTLFMGVPRIWEKMqdtikenvarssrlrkkafawakmlglkvntkrmlgkrdipMN 370
Cdd:pfam00501 229 VVLPPGFPALdpAALLELIERYKVTVLYGVPTLLNML-----------------------------------------LE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 371 YRMAKALVFAKVRTslgldnchaFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSGPHTVS---NKSVYRVLSCGKVL 446
Cdd:pfam00501 268 AGAPKRALLSSLRL---------VLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSVGRPL 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000640 447 SGCKNMLYNQNKEG------VGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITA 519
Cdd:pfam00501 339 PGTEVKIVDDETGEpvppgePGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
73-535 |
3.26e-84 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 272.17 E-value: 3.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 73 KWdtLTFSQYYEMCRKAAKSLIKLGLQRF--QCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVS 150
Cdd:cd05927 4 EW--ISYKEVAERADNIGSALRSLGGKPApaSFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 151 ILIVENDqqlqkillippdkmetVKaivqyklplmesmanLYSWNDFMELG--NDIPNIQldrvilsQKANQCAVILYTS 228
Cdd:cd05927 82 IVFCDAG----------------VK---------------VYSLEEFEKLGkkNKVPPPP-------PKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 229 GTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNTIVSYLPLSHI---AAQLTDIWIPIKIGaltFFAQPDALrgtL 305
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIferVVEALFLYHGAKIG---FYSGDIRL---L 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 306 VYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAkmlglkVNTKRMLGKRDIPMNYRMAKALVFAKVRTS 385
Cdd:cd05927 198 LDDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFA------LNYKLAELRSGVVRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 386 LGLdNCHAFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCK-------NMLYNQN 457
Cdd:cd05927 272 LGG-NVRLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEvklvdvpEMNYDAK 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000640 458 KE-GVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKE 535
Cdd:cd05927 351 DPnPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYAR 429
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
49-547 |
2.39e-70 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 233.16 E-value: 2.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 49 IPELFQESAERFSAYPALASKngkkWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLC 128
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 129 VGIYATNSAEACQYVIQQANVSILIvendqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniq 208
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 209 ldrvilsqkanqCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIAAQLTDIWIPIK 288
Cdd:COG0318 102 ------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP----GDVVLVALPLFHVFGLTVGLLAPLL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 289 IGA-LTFFAQPDALRgtLVYTLQEVKPTLFMGVPRIWekmqdtikenvarssrlrkkafawakmlglkvntkrmlgkrdi 367
Cdd:COG0318 166 AGAtLVLLPRFDPER--VLELIERERVTVLFGVPTML------------------------------------------- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 368 pmnYRMAKALVFAKVRTSlGLdncHAFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSGPHTVS--NKSVYRVLSCGK 444
Cdd:COG0318 201 ---ARLLRHPEFARYDLS-SL---RLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 445 VLSGCKNMLYNQNKE-----GVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITa 519
Cdd:COG0318 274 PLPGVEVRIVDEDGRelppgEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS- 351
|
490 500
....*....|....*....|....*...
gi 569000640 520 GGENVSPIPIETLVKEkIPIISHAMLVG 547
Cdd:COG0318 352 GGENVYPAEVEEVLAA-HPGVAEAAVVG 378
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
74-559 |
9.72e-68 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 229.62 E-value: 9.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 74 WDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILI 153
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 154 VENDQQLQKILLIpPDKMETVKAIV--------QYKLPLMESMAnlyswnDFMELGNDI----PNIqLDRVILSQKANQC 221
Cdd:cd17641 89 AEDEEQVDKLLEI-ADRIPSVRYVIycdprgmrKYDDPRLISFE------DVVALGRALdrrdPGL-YEREVAAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNItwtagaMSQEMEINRVSGKQNT--IVSYLPLSHIAAQLTDIWIPIKIG-ALTFFAQP 298
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNF------LGHCAAYLAADPLGPGdeYVSVLPLPWIGEQMYSVGQALVCGfIVNFPEEP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 299 DalrgTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRMLGKR---DIPMNYRMAK 375
Cdd:cd17641 235 E----TMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPvslWLRLASWLAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 376 ALVFAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYN 455
Cdd:cd17641 311 ALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 456 qnkegVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKE 535
Cdd:cd17641 391 -----VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKF 465
|
490 500
....*....|....*....|....
gi 569000640 536 KiPIISHAMLVGDKAKFLCMLLTL 559
Cdd:cd17641 466 S-PYIAEAVVLGAGRPYLTAFICI 488
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
71-530 |
2.51e-67 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 226.97 E-value: 2.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 71 GKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVS 150
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 151 ILIVENdqqlqkilLIPPDKMETVKA--IVQYKLPLMESMANLYSWNDFMELGNdiPNIQLDRvilsQKANQCAVILYTS 228
Cdd:cd05932 81 ALFVGK--------LDDWKAMAPGVPegLISISLPPPSAANCQYQWDDLIAQHP--PLEERPT----RFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 229 GTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPdalRGTLVYT 308
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGIEHIGTE----ENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES---LDTFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 309 LQEVKPTLFMGVPRIWEKMQDTI--KENVARSSRLRKkafawakmlglkvntkrmlgkrdIPMnyrmAKALVFAKVRTSL 386
Cdd:cd05932 220 VQRARPTLFFSVPRLWTKFQQGVqdKIPQQKLNLLLK-----------------------IPV----VNSLVKRKVLKGL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 387 GLDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQnkegvGEVCM 466
Cdd:cd05932 273 GLDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILV 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000640 467 WGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIE 530
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIE 411
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
81-553 |
3.36e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 217.31 E-value: 3.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 81 QYYEMCRKAAKSLIKL---GLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEND 157
Cdd:cd05914 9 TYKDLADNIAKFALLLkinGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 158 QQLqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkanqcAVILYTSGTTGTPKGV 237
Cdd:cd05914 89 DDV-------------------------------------------------------------ALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 238 LLSHDNITWTAGAMSqEMEInrvSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAqpDALRGTLVYTLQEVKPTLF 317
Cdd:cd05914 108 MLTYRNIVSNVDGVK-EVVL---LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 318 MGVPRIWEKMQDTIKENVArssrlrkkafawakmlglKVNTKRMLGKRDIPMNYRMAKALVFAKVRTSLGlDNCHAFFSS 397
Cdd:cd05914 182 LGVPVPLVIEKIFKMDIIP------------------KLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 398 ASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQN-KEGVGEVCMWGRHVFMGYL 476
Cdd:cd05914 243 GAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYY 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000640 477 NKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIET-LVKEKIPIISHAMLVGDKAKFL 553
Cdd:cd05914 323 KNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLESLVVVQEKKLVAL 400
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
75-547 |
9.72e-62 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 211.30 E-value: 9.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 ENDQqLQKIL-----LIPPDKMETVKAIVQYKLPLMESmanlyswnDFMELGNDIPNIQLDRVilsQKANQCAVILYTSG 229
Cdd:cd05911 89 DPDG-LEKVKeaakeLGPKDKIIVLDDKPDGVLSIEDL--------LSPTLGEEDEDLPPPLK---DGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 230 TTGTPKGVLLSHDNITwtAGAMSQEMEINRVSGKQNTIVSYLPLSHIAaqltdiwipikiGALTFFAQPdaLRGTLVYTL 309
Cdd:cd05911 157 TTGLPKGVCLSHRNLI--ANLSQVQTFLYGNDGSNDVILGFLPLYHIY------------GLFTTLASL--LNGATVIIM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 310 QEVKPTLFMgvpriwekmqDTIKENvarssrlrKKAFAW---AKMLglkvntkrMLGKRDIPMNYRMAkalvfakvrtSL 386
Cdd:cd05911 221 PKFDSELFL----------DLIEKY--------KITFLYlvpPIAA--------ALAKSPLLDKYDLS----------SL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 387 gldncHAFFSSASPLSQDVSEFfLSLDIPIGEI---YGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYN------QN 457
Cdd:cd05911 265 -----RVILSGGAPLSKELQEL-LAKRFPNATIkqgYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDddgkdsLG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 458 KEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKEkI 537
Cdd:cd05911 339 PNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAVLLE-H 416
|
490
....*....|
gi 569000640 538 PIISHAMLVG 547
Cdd:cd05911 417 PGVADAAVIG 426
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
24-548 |
1.89e-60 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 211.88 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 24 WSTHCDGEVLLRLSKHGPGHETPMTIPELFQESAERFSAYPALASK---NGK----KWdtLTFSQYYEMcRKAAKS-LIK 95
Cdd:PLN02736 21 WNVYRSARSPLKLVSRFPDHPEIGTLHDNFVYAVETFRDYKYLGTRirvDGTvgeyKW--MTYGEAGTA-RTAIGSgLVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 96 LGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVeNDQQLQKILLIPPDkMETVK 175
Cdd:PLN02736 98 HGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE-IPSVR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 176 AIVQY-----KLPLMESMAN--LYSWNDFMELGNDIPniqldRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTA 248
Cdd:PLN02736 176 LIVVVggadePLPSLPSGTGveIVTYSKLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 249 GAMSQEMEInrvsGKQNTIVSYLPLSHI---AAQLTDIWIPIKIGaltfFAQPDALRgtLVYTLQEVKPTLFMGVPRIWE 325
Cdd:PLN02736 251 AGSSLSTKF----YPSDVHISYLPLAHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSVPRLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 326 KMQDTIKENVARSSRLRKKAFAWAkmlglkVNTKR---MLGKRDIPMNYRmakaLVFAKVRTSLGlDNCHAFFSSASPLS 402
Cdd:PLN02736 321 RIYDGITNAVKESGGLKERLFNAA------YNAKKqalENGKNPSPMWDR----LVFNKIKAKLG-GRVRFMSSGASPLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 403 QDVSEFflsLDIPIG----EIYGMSECSGPHTVSNKSVYrvlSCGKVLS---GCK-------NMLYNQNKEGV--GEVCM 466
Cdd:PLN02736 390 PDVMEF---LRICFGgrvlEGYGMTETSCVISGMDEGDN---LSGHVGSpnpACEvklvdvpEMNYTSEDQPYprGEICV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 467 WGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETlVKEKIPIISHAMLV 546
Cdd:PLN02736 464 RGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFVY 542
|
..
gi 569000640 547 GD 548
Cdd:PLN02736 543 GD 544
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
76-551 |
4.96e-58 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 202.06 E-value: 4.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelGNDIpniqldrvilsqkanqcAVILYTSGTTGTPK 235
Cdd:cd17639 85 GK-------------------------------------------PDDL-----------------ACIMYTSGSTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 236 GVLLSHDNITwtAGAMSQEMEINRVSGKQNTIVSYLPLSHI---AAQLTDIWIPIKIGaltfFAQPDalrgTLVYT---- 308
Cdd:cd17639 105 GVMLTHGNLV--AGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAENVCLYRGGTIG----YGSPR----TLTDKskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 309 ----LQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFawakmlglkvntkrmlgkrDIPMNYRMAK--------- 375
Cdd:cd17639 175 ckgdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLF-------------------WTAYQSKLKAlkegpgtpl 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 376 --ALVFAKVRTSLGlDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNML 453
Cdd:cd17639 236 ldELVFKKVRAALG-GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 --------YNQNKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVS 525
Cdd:cd17639 315 vdweeggySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIA 394
|
490 500
....*....|....*....|....*.
gi 569000640 526 PIPIETLVKEKiPIISHAMLVGDKAK 551
Cdd:cd17639 395 LEKLESIYRSN-PLVNNICVYADPDK 419
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
220-547 |
1.41e-57 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 195.97 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 220 QCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIAaQLTDIWIPIKIGA-LTFFAQP 298
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE----GDVFLSTLPLFHIG-GLFGLLGALLAGGtVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 299 DAlrGTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRkkafawakmlglkvntkrmlgkrdipmnyrmakalv 378
Cdd:cd04433 76 DP--EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLR------------------------------------ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 379 fakvrtslgldnchAFFSSASPLSQDVSEFFLSL-DIPIGEIYGMSECSGPHTVSNK--SVYRVLSCGKVLSGCKNMLYN 455
Cdd:cd04433 118 --------------ALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPddDARKPGSVGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 456 QNKE-----GVGEVCMWGRHVFMGYLNKEEATlEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:cd04433 184 PDGGelppgEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVE 261
|
330
....*....|....*..
gi 569000640 531 TLVkEKIPIISHAMLVG 547
Cdd:cd04433 262 AVL-LGHPGVAEAAVVG 277
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
76-553 |
9.35e-52 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 184.10 E-value: 9.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelGNDIpniqldrvilsqkanqcAVILYTSGTTGTPK 235
Cdd:cd17640 85 ND-------------------------------------------SDDL-----------------ATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 236 GVLLSHDNITWTagaMSQEMEInrVSGKQNTIV-SYLPLSHIAAQLTDIWIPIKIGALTFFAQPdalrgTLVYTLQEVKP 314
Cdd:cd17640 105 GVMLTHANLLHQ---IRSLSDI--VPPQPGDRFlSILPIWHSYERSAEYFIFACGCSQAYTSIR-----TLKDDLKRVKP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 315 TLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKvntkrmlgkrdipmnyrmaKALVfakvrtslgldnchaf 394
Cdd:cd17640 175 HYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGIF-------------------KFGI---------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 395 fSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQNKEGV------GEVCMWG 468
Cdd:cd17640 220 -SGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 469 RHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETlVKEKIPIISHAMLVGD 548
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEE-ALMRSPFIEQIMVVGQ 377
|
....*
gi 569000640 549 KAKFL 553
Cdd:cd17640 378 DQKRL 382
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
51-568 |
1.43e-51 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 187.54 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASK---NGK--KWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PLN02614 49 DVFRMSVEKYPNNPMLGRReivDGKpgKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGIYATNSAEACQYVIQQANVSILIVEnDQQLQKILLIPPDKMETVKAIVQYK--LPLMESMAN-----LYSWNDFM 198
Cdd:PLN02614 129 LYCVPLYDTLGAGAVEFIISHSEVSIVFVE-EKKISELFKTCPNSTEYMKTVVSFGgvSREQKEEAEtfglvIYAWDEFL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 199 ELGN----DIPniqldrviLSQKANQCaVILYTSGTTGTPKGVLLSHDNI-TWTAGAMSQEMEINRVSGKQNTIVSYLPL 273
Cdd:PLN02614 208 KLGEgkqyDLP--------IKKKSDIC-TIMYTSGTTGDPKGVMISNESIvTLIAGVIRLLKSANAALTVKDVYLSYLPL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 274 SHIAAQLTDIWIpIKIGALTFFAQPDAlrGTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAF--AWAKM 351
Cdd:PLN02614 279 AHIFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFdsAFSYK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 352 LGlkvNTKRmlGKRDIPMNYRMAKaLVFAKVRTSLGlDNCHAFFSSASPLSQDVSEFFLSLD-IPIGEIYGMSE-CSGPH 429
Cdd:PLN02614 356 FG---NMKK--GQSHVEASPLCDK-LVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTEsCAGTF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 430 TVSNKSVYRVLSCGKV-------LSGCKNMLYNQ-NKEGVGEVCMWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLD 501
Cdd:PLN02614 429 VSLPDELDMLGTVGPPvpnvdirLESVPEMEYDAlASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQ 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 502 SHDFLYITGRIKEILITAGGENVSPIPIETLVKEkIPIISHAMLVGDkaKFLCMLLTLKDRHQNLRE 568
Cdd:PLN02614 508 PNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGE-VQAVDSVWVYGN--SFESFLVAIANPNQQILE 571
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
76-532 |
3.33e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 184.02 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSIlIVE 155
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKA-IVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDQQLQKIL-LIPPDKMETVKAIVQYKLPL---MESMaNLYSWNDFMELG-----NDIPNIQLDRvilsqkaNQCAVILY 226
Cdd:PTZ00216 200 NGKNVPNLLrLMKSGGMPNTTIIYLDSLPAsvdTEGC-RLVAWTDVVAKGhsagsHHPLNIPENN-------DDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 227 TSGTTGTPKGVLLSHDNITwtAGAMSQEMEINRVSGK---QNTIVSYLPLSHIAaQLTDIWIPIKIGALTFFAQPDAL-- 301
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLT--AGILALEDRLNDLIGPpeeDETYCSYLPLAHIM-EFGVTNIFLARGALIGFGSPRTLtd 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 -----RGTLVytlqEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAF--AWAKML-GLKVntkrmlGKrDIPmnYRM 373
Cdd:PTZ00216 349 tfarpHGDLT----EFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFdhAYQSRLrALKE------GK-DTP--YWN 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 374 AKalVFAKVRTSLGlDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSEcsgphTVSNKSVYRV--LSC---GKVLSG 448
Cdd:PTZ00216 416 EK--VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTE-----TVCCGGIQRTgdLEPnavGQLLKG 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 449 CKNML-------YNQNKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGG 521
Cdd:PTZ00216 488 VEMKLldteeykHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLG 567
|
490
....*....|.
gi 569000640 522 ENvspIPIETL 532
Cdd:PTZ00216 568 EY---IALEAL 575
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
46-530 |
4.01e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 177.79 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 46 PMTIPELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGIYATNSAEACQYVIQQANVSILIVEndQQLQKILLIPPDKMETVKAIVQYKLP-LMESMANLYSWNDFMELGNDi 204
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFVL--GLFLGVDYSATTRLPALEHVVICETEeDDPHTEKMKTFTDFLAAGDP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 205 pniqlDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIAAqLTDIW 284
Cdd:PRK07656 157 -----AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTE----GDRYLAANPFFHVFG-YKAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 285 I-PIKIGAlTFFAQP--DALRgtLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRkkafawakmlgLKVNtkrm 361
Cdd:PRK07656 227 NaPLMRGA-TILPLPvfDPDE--VFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLR-----------LAVT---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 362 lGKRDIPMNY--RMAKALVFAKVRTSlgldnchaffssasplsqdvsefflsldipigeiYGMSECSGPHTVSNKSVYRV 439
Cdd:PRK07656 289 -GAASMPVALleRFESELGVDIVLTG----------------------------------YGLSEASGVTTFNRLDDDRK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 440 L---SCGKVLSGCKNMLYNQNKEG-----VGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGR 511
Cdd:PRK07656 334 TvagTIGTAIAGVENKIVNELGEEvpvgeVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDR 413
|
490
....*....|....*....
gi 569000640 512 IKEILITaGGENVSPIPIE 530
Cdd:PRK07656 414 KKDMFIV-GGFNVYPAEVE 431
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
77-525 |
1.11e-47 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 176.57 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVvTALGTILAGGLC-VGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWI-IAMEACNSQGITyVPLYDTLGANAVEFIINHAEVSIAFVQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 nDQQLQKILLIPPDKMETVKAIVQY-------KLPLMESMANLYSWNDFMELGN---DIPNiqldrvilSQKANQCAvIL 225
Cdd:PLN02861 157 -ESKISSILSCLPKCSSNLKTIVSFgdvsseqKEEAEELGVSCFSWEEFSLMGSldcELPP--------KQKTDICT-IM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 226 YTSGTTGTPKGVLLSHDNITwtAGAMSQE---MEINRVSGKQNTIVSYLPLSHIAAQLTDIWIpIKIGALTFFAQPDaLR 302
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAII--AEVLSTDhllKVTDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGD-IR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 303 gTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRMLGKRDIPMNYRmakaLVFAKV 382
Cdd:PLN02861 303 -YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEASPRLDR----LVFDKI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 383 RTSLGlDNCHAFFSSASPLSQDVSEFFLSLDIP-IGEIYGMSE-CSGPHTvsnkSVYRVLS-CGKV----------LSGC 449
Cdd:PLN02861 378 KEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTEsCGGCFT----SIANVFSmVGTVgvpmttiearLESV 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 450 KNMLYNQ-NKEGVGEVCMWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVS 525
Cdd:PLN02861 453 PEMGYDAlSDVPRGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVA 528
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
36-551 |
7.29e-47 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 174.23 E-value: 7.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 36 LSKHG-PGHETPMTIP-ELFQESAERFSAYPALA---SKNGK----KWDTltFSQYYEMCRKAAKSLIKLGLQRFQCVGI 106
Cdd:PLN02430 29 LSKKGfPPIDSDITTAwDIFSKSVEKYPDNKMLGwrrIVDGKvgpyMWKT--YKEVYEEVLQIGSALRASGAEPGSRVGI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 107 LGFNSVEWVVtALGTILAGGL-CVGIYATNSAEACQYVIQQANVSILIVEnDQQLQKILliPPD--KMETVKAIVQYKLP 183
Cdd:PLN02430 107 YGSNCPQWIV-AMEACAAHSLiCVPLYDTLGPGAVDYIVDHAEIDFVFVQ-DKKIKELL--EPDckSAKRLKAIVSFTSV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 184 LMESM-------ANLYSWNDFMELGNDIPNiqldrVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEME 256
Cdd:PLN02430 183 TEEESdkasqigVKTYSWIDFLHMGKENPS-----ETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFME 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 257 inRVSGKQNT---IVSYLPLSHIAAQLTDIWIPIKIGALTFF-AQPDALRGTLvytlQEVKPTLFMGVPRIWEKMQDTIK 332
Cdd:PLN02430 258 --QFEDKMTHddvYLSFLPLAHILDRMIEEYFFRKGASVGYYhGDLNALRDDL----MELKPTLLAGVPRVFERIHEGIQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 333 ENVARSSRLRKKAFawakmlglKVNTKRMLGKRDIPMNYR----MAKALVFAKVRTSLGlDNCHAFFSSASPLSQDVSEF 408
Cdd:PLN02430 332 KALQELNPRRRLIF--------NALYKYKLAWMNRGYSHKkaspMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 409 F-LSLDIPIGEIYGMSECSGPH------------TVSNKSVYRVLSCGKVlsgcKNMLYNQNKEG-VGEVCMWGRHVFMG 474
Cdd:PLN02430 403 LrVTSCAFVVQGYGLTETLGPTtlgfpdemcmlgTVGAPAVYNELRLEEV----PEMGYDPLGEPpRGEICVRGKCLFSG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 475 YLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSpipIETLvkEKI----PIISHAMLVGDKA 550
Cdd:PLN02430 479 YYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVA---LEYL--ENVygqnPIVEDIWVYGDSF 552
|
.
gi 569000640 551 K 551
Cdd:PLN02430 553 K 553
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
49-530 |
2.00e-46 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 169.28 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 49 IPELFQESAERFSAYPALAskNGKKWdtLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLC 128
Cdd:cd05936 1 LADLLEEAARRFPDKTALI--FMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 129 VgiyatnsaeacqyviqqaNVSILIVEndQQLQKILlippdKMETVKAIVQyklplmesmanLYSWNDFMELGNDIPniq 208
Cdd:cd05936 77 V------------------PLNPLYTP--RELEHIL-----NDSGAKALIV-----------AVSFTDLLAAGAPLG--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 209 lDRVILSqkANQCAVILYTSGTTGTPKGVLLSHDNITwtAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIK 288
Cdd:cd05936 118 -ERVALT--PEDVAVLQYTSGTTGVPKGAMLTHRNLV--ANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 289 IGA-LTFFAQPDALRgtLVYTLQEVKPTLFMGVPRIWEKMqdtikenvarssrlrkkafawakmlglkvntkrmlgkrdi 367
Cdd:cd05936 193 LGAtIVLIPRFRPIG--VLKEIRKHRVTIFPGVPTMYIAL---------------------------------------- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 368 pMNYRMAKALVFAKVRTSLgldnchaffSSASPLSQDVSEFFLSL-DIPIGEIYGMSECSgPHTVSNKS--VYRVLSCGK 444
Cdd:cd05936 231 -LNAPEFKKRDFSSLRLCI---------SGGAPLPVEVAERFEELtGVPIVEGYGLTETS-PVVAVNPLdgPRKPGSIGI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 445 VLSGCKNMLYNQNKE----G-VGEVCMWGRHVFMGYLNKEEATLEALDeNGWLHSGDIGRLDSHDFLYITGRIKEILItA 519
Cdd:cd05936 300 PLPGTEVKIVDDDGEelppGeVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-V 377
|
490
....*....|.
gi 569000640 520 GGENVSPIPIE 530
Cdd:cd05936 378 GGFNVYPREVE 388
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
44-525 |
5.65e-46 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 172.22 E-value: 5.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 44 ETP----MTIPELFQESAERFSAYPAL-----------ASKNGKKWDTLTFSQY--------YEMCRKAAKSLIKLGLQR 100
Cdd:PLN02387 51 ETPwegaTTLAALFEQSCKKYSDKRLLgtrklisrefeTSSDGRKFEKLHLGEYewitygqvFERVCNFASGLVALGHNK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 101 FQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENdQQLQKILLIPpDKMETVKAIV-- 178
Cdd:PLN02387 131 EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS-KQLKKLIDIS-SQLETVKRVIym 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 179 ----QYKLPLMESMAN--LYSWNDFMELGNDIPnIQLDRvilsQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMs 252
Cdd:PLN02387 209 ddegVDSDSSLSGSSNwtVSSFSEVEKLGKENP-VDPDL----PSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGV- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 253 qeMEINRVSGKQNTIVSYLPLSHI---AAQLTDIWIPIKIG---ALTFFAQPDAL-RGTLvYTLQEVKPTLFMGVPRIWE 325
Cdd:PLN02387 283 --MTVVPKLGKNDVYLAYLPLAHIlelAAESVMAAVGAAIGygsPLTLTDTSNKIkKGTK-GDASALKPTLMTAVPAILD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 326 KMQDTIKENVARSSRLRKKAF--AWAKMLGlKVN--------TKRMLGkrdipmnyrmaKALVFAKVRTSLGlDNCHAFF 395
Cdd:PLN02387 360 RVRDGVRKKVDAKGGLAKKLFdiAYKRRLA-AIEgswfgawgLEKLLW-----------DALVFKKIRAVLG-GRIRFML 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 396 SSASPLSQDVSEFF-LSLDIPIGEIYGMSE-CSGPhTVSN---KSVYRVlscGKVLSGCKNMLYNQNKEGV--------- 461
Cdd:PLN02387 427 SGGAPLSGDTQRFInICLGAPIGQGYGLTEtCAGA-TFSEwddTSVGRV---GPPLPCCYVKLVSWEEGGYlisdkpmpr 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000640 462 GEVCMWGRHVFMGYLNKEEATLEA--LDENG--WLHSGDIGRLDSHDFLYITGRIKEILITAGGENVS 525
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVS 570
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
76-530 |
9.79e-46 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 166.63 E-value: 9.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIve 155
Cdd:cd17631 20 SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 ndqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgNDIpniqldrvilsqkanqcAVILYTSGTTGTPK 235
Cdd:cd17631 98 ----------------------------------------------DDL-----------------ALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 236 GVLLSHDNITWTAgaMSQEMEINrVSGKQNTIVSyLPLSHIAAQLTdIWIPI--KIGALTFFAQPDAlrGTLVYTLQEVK 313
Cdd:cd17631 115 GAMLTHRNLLWNA--VNALAALD-LGPDDVLLVV-APLFHIGGLGV-FTLPTllRGGTVVILRKFDP--ETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 314 PTLFMGVPRIWEKMQDTIKENVARSSRLRkkafawakmlglkvntkrmlgkrdipmnyrmakalvfakvrtslgldnchA 393
Cdd:cd17631 188 VTSFFLVPTMIQALLQHPRFATTDLSSLR--------------------------------------------------A 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 394 FFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTV--SNKSVYRVLSCGKVLSGCKNMLYNQNKE-----GVGEVCM 466
Cdd:cd17631 218 VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVV 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000640 467 WGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:cd17631 298 RGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
46-530 |
1.30e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 168.44 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 46 PMTIPELFQESAERFSAYPALASkNGKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYF-DGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GlcvgIYAT-N---SAEACQYVIQQANVSILIVEND--QQLQKILlippDKMETVKAIVQYK-LPLMESMANLYSWNDFM 198
Cdd:PRK06187 81 A----VLHPiNirlKPEEIAYILNDAEDRVVLVDSEfvPLLAAIL----PQLPTVRTVIVEGdGPAAPLAPEVGEYEELL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 199 ELGND-IPNIQLDrvilsqkANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIA 277
Cdd:PRK06187 153 AAASDtFDFPDID-------ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR----DDVYLVIVPMFHVH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 278 AqltdIWIPIkigaLTFFA----------QPDALrgtLVYTLQEvKPTLFMGVPRIWekmqdtikenvarssrlrkkafa 347
Cdd:PRK06187 222 A----WGLPY----LALMAgakqviprrfDPENL---LDLIETE-RVTFFFAVPTIW----------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 348 wakmlglkvntkRMLgkrdipMNYRMAKALVFAKVRtslgldnchAFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECS 426
Cdd:PRK06187 267 ------------QML------LKAPRAYFVDFSSLR---------LVIYGGAALPPALLREFKEkFGIDLVQGYGMTETS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 427 G-------PHTVSNKSVYRvLSCGKVLSGCK--------NMLYNQNKEgVGEVCMWGRHVFMGYLNKEEATLEALDeNGW 491
Cdd:PRK06187 320 PvvsvlppEDQLPGQWTKR-RSAGRPLPGVEarivdddgDELPPDGGE-VGEIIVRGPWLMQGYWNRPEATAETID-GGW 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 569000640 492 LHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:PRK06187 397 LHTGDVGYIDEDGYLYITDRIKDVIIS-GGENIYPRELE 434
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
64-530 |
1.68e-44 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 164.79 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 64 PALASKNGKKWdtLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIyatNSAeacqyv 143
Cdd:cd05926 4 PALVVPGSTPA--LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPL---NPA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 144 IQQANVSILIVENDQqlqKILLIPPDK-METVKAIVQYKLPLMEsMANLYSWNDFMELGNDIPNIQLDRVILSQ----KA 218
Cdd:cd05926 73 YKKAEFEFYLADLGS---KLVLTPKGElGPASRAASKLGLAILE-LALDVGVLIRAPSAESLSNLLADKKNAKSegvpLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 219 NQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgKQNTIVsYLPLSHI----AAQLTDI------WIPIK 288
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTP---DDRTLV-VMPLFHVhglvASLLSTLaaggsvVLPPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 289 IGALTFFAQpdalrgtlvytLQEVKPTLFMGVPRIwekmqdtikenvarssrlrkkafawakmlglkvntKRMLGKRDIP 368
Cdd:cd05926 225 FSASTFWPD-----------VRDYNATWYTAVPTI-----------------------------------HQILLNRPEP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 369 MNYRMAKALVFakVRtslgldnchaffSSASPLSQDV-SEFFLSLDIPIGEIYGMSECSGPHTvSNK---SVYRVLSCGK 444
Cdd:cd05926 259 NPESPPPKLRF--IR------------SCSASLPPAVlEALEATFGAPVLEAYGMTEAAHQMT-SNPlppGPRKPGSVGK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 445 VlSGCKNMLYNQNKE-----GVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEIlITA 519
Cdd:cd05926 324 P-VGVEVRILDEDGEilppgVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL-INR 401
|
490
....*....|.
gi 569000640 520 GGENVSPIPIE 530
Cdd:cd05926 402 GGEKISPLEVD 412
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
48-530 |
9.96e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 141.06 E-value: 9.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKN-GKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGG 126
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHqALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 127 LCVGIYATNSAEACQYVIQQANVSILIV-----ENDQQLQKILLIPPDKMETVKAIVQYKLPLME---SMA-----NLYS 193
Cdd:PRK12583 96 ILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGALACERLPELRgvvSLApapppGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 194 WNDFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPL 273
Cdd:PRK12583 176 WHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGL----TEHDRLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 274 SHIAAQLTDIWIPIKIGALTFFAQ----PDAlrgtlvyTLQEV---KPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAF 346
Cdd:PRK12583 252 YHCFGMVLANLGCMTVGACLVYPNeafdPLA-------TLQAVeeeRCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 347 AWAKMLgLKVnTKRMLGKRDIPmnyrmakalvfakvrtslgldnchaffssasplsqdvsefflslDIPIGeiYGMSECS 426
Cdd:PRK12583 325 AGAPCP-IEV-MRRVMDEMHMA--------------------------------------------EVQIA--YGMTETS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 427 gP----HTVSNKSVYRVLSCGKVLSGCKNMLYNQNKEGV-----GEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDI 497
Cdd:PRK12583 357 -PvslqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVprgeiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDL 435
|
490 500 510
....*....|....*....|....*....|...
gi 569000640 498 GRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:PRK12583 436 ATMDEQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
47-530 |
2.72e-35 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 139.56 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 47 MTIPELFQESAERFSAYPALASKN-GKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDqGLRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGI---YATNSAEacqYVIQQANVSILIV-----END--QQLQKilLIPPDKMETVKAIVQYKLPLMESM------- 188
Cdd:PRK08315 93 AILVTInpaYRLSELE---YALNQSGCKALIAadgfkDSDyvAMLYE--LAPELATCEPGQLQSARLPELRRViflgdek 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 189 -ANLYSWNDFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNIT----WTAGAMSqemeinrvSGK 263
Cdd:PRK08315 168 hPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngyFIGEAMK--------LTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 264 QNTIVSYLPLSH----IAAQLtdiwipikiGALTFFAqpdalrgTLVY---------TLQEVK----------PTLFMGV 320
Cdd:PRK08315 240 EDRLCIPVPLYHcfgmVLGNL---------ACVTHGA-------TMVYpgegfdplaTLAAVEeerctalygvPTMFIAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 321 ---PRIweKMQDTikenvarsSRLRkkafawakmlglkvnTKRMLGkrdipmnyrmakalvfakvrtslgldnchaffsS 397
Cdd:PRK08315 304 ldhPDF--ARFDL--------SSLR---------------TGIMAG---------------------------------S 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 398 ASP---LSQDVSEFFLSlDIPIGeiYGMSECSgPhtVSNKSV------YRVLSCGKVLSGC--KNMLYNQNKE---GV-G 462
Cdd:PRK08315 326 PCPievMKRVIDKMHMS-EVTIA--YGMTETS-P--VSTQTRtddpleKRVTTVGRALPHLevKIVDPETGETvprGEqG 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000640 463 EVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:PRK08315 400 ELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE 466
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
75-547 |
1.04e-34 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 136.27 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLI-KLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILi 153
Cdd:cd05941 10 DSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 154 vendqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqLDRvilsqkanqcAVILYTSGTTGT 233
Cdd:cd05941 89 -------------------------------------------------------LDP----------ALILYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 234 PKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIAAQLTDIWIPIKIGA----LTFF-AQPDALRgtlvyt 308
Cdd:cd05941 104 PKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNALLCPLFAGAsvefLPKFdPKEVAIS------ 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 309 lQEVKP-TLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAwakmlglkvntkrmlgkrdipmnyrmakalvfaKVRTslg 387
Cdd:cd05941 174 -RLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAE---------------------------------RLRL--- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 388 ldnchaFFSSASPLSQDVSEFFLSLD-IPIGEIYGMSECSgpHTVSN--KSVYRVLSCGKVLSGCKNMLYNQN------K 458
Cdd:cd05941 217 ------MVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG--MALSNplDGERRPGTVGMPLPGVQARIVDEEtgeplpR 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 459 EGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKEkIP 538
Cdd:cd05941 289 GEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLA-HP 367
|
....*....
gi 569000640 539 IISHAMLVG 547
Cdd:cd05941 368 GVSECAVIG 376
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
55-542 |
1.59e-33 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 133.90 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 55 ESAERFSAYPALA-SKNGkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYA 133
Cdd:cd05904 13 LFASAHPSRPALIdAATG---RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 134 TNSAEACQYVIQQANVSILIVENdqqlqkillippdkmETVKAIVQYKLP--LMESMANLYSWNDfmELGNDIPNIQLDR 211
Cdd:cd05904 90 LSTPAEIAKQVKDSGAKLAFTTA---------------ELAEKLASLALPvvLLDSAEFDSLSFS--DLLFEADEAEPPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 212 VILSQkaNQCAVILYTSGTTGTPKGVLLSHDNITwtAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAqltdiwipikiga 291
Cdd:cd05904 153 VVIKQ--DDVAALLYSSGTTGRSKGVMLTHRNLI--AMVAQFVAGEGSNSDSEDVFLCVLPMFHIYG------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 292 LTFFAQ-PDALRGTLVytlqeVKPTLFMgvpriwEKMQDTIKEnvarssrlRKKAFAWAK---MLGLKvntkrmlgKRDI 367
Cdd:cd05904 216 LSSFALgLLRLGATVV-----VMPRFDL------EELLAAIER--------YKVTHLPVVppiVLALV--------KSPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 368 PMNYRmakalvFAKVRTSLgldnchaffSSASPLSQDVSEFFLSL--DIPIGEIYGMSECSGP-HTVSN--KSVYRVLSC 442
Cdd:cd05904 269 VDKYD------LSSLRQIM---------SGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFApeKDRAKYGSV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 443 GKVLSGCKNML----------YNQnkegVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRI 512
Cdd:cd05904 334 GRLVPNVEAKIvdpetgeslpPNQ----TGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRL 409
|
490 500 510
....*....|....*....|....*....|
gi 569000640 513 KEiLITAGGENVSPIPIETLvkekipIISH 542
Cdd:cd05904 410 KE-LIKYKGFQVAPAELEAL------LLSH 432
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
48-525 |
1.14e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.59 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGD----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGI-YATNSAEACqYVIQQANVSILIVEND--QQLQKILlippDKMETVKAIVQYKLPLMESMANLYSWNDFMELGND- 203
Cdd:PRK08316 88 HVPVnFMLTGEELA-YILDHSGARAFLVDPAlaPTAEAAL----ALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 204 IPNIQLDRVILSQkanqcavILYTSGTTGTPKGVLLSHDNITW------TAGAMSQEmeinrvsgkqNTIVSYLPLSHiA 277
Cdd:PRK08316 163 EPDVELADDDLAQ-------ILYTSGTESLPKGAMLTHRALIAeyvsciVAGDMSAD----------DIPLHALPLYH-C 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 278 AQLTDIWIP-IKIGALTFFAQ-PDAlrGTLVYTLQEVKPTLFMGVPRIWekmqdtIkenvarsSRLRKKAFAWAKMLGLk 355
Cdd:PRK08316 225 AQLDVFLGPyLYVGATNVILDaPDP--ELILRTIEAERITSFFAPPTVW------I-------SLLRHPDFDTRDLSSL- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 356 vnTKRMLGKRDIPMNY--RMAKALvfakvrTSLGLDNChaffssasplsqdvsefflsldipigeiYGMSECSGPHTVSN 433
Cdd:PRK08316 289 --RKGYYGASIMPVEVlkELRERL------PGLRFYNC----------------------------YGQTEIAPLATVLG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 434 --KSVYRVLSCGK-VLsgckNM---LYNQNKEGV-----GEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDS 502
Cdd:PRK08316 333 peEHLRRPGSAGRpVL----NVetrVVDDDGNDVapgevGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDE 407
|
490 500
....*....|....*....|...
gi 569000640 503 HDFLYITGRIKEILITaGGENVS 525
Cdd:PRK08316 408 EGYITVVDRKKDMIKT-GGENVA 429
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
38-547 |
2.62e-31 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 127.64 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 38 KHGPGHETPM---TIPELFQESAERFSAYP-ALASKNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVE 113
Cdd:cd17642 2 IVGPGPFYPLedgTAGEQLHKAMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 114 WVVTALGTILAGglcVGIYATNSAEACQYVIQQANVS--ILIVENDQQLQKILLIPpDKMETVKAIVqyKLPLMESMANL 191
Cdd:cd17642 82 FFLPVIAGLFIG---VGVAPTNDIYNERELDHSLNISkpTIVFCSKKGLQKVLNVQ-KKLKIIKTII--ILDSKEDYKGY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 192 YSWNDFMElGNDIPNIQLDRVILSQ--KANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSgKQNTIVS 269
Cdd:cd17642 156 QCLYTFIT-QNLPPGFNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQII-PDTAILT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 270 YLPLSHIAAQLTdiwipiKIGALTFfaqpdALRGTLVYTLQEvkpTLFMgvpriwekmqDTIKENVARSSRLRKKAFAWa 349
Cdd:cd17642 234 VIPFHHGFGMFT------TLGYLIC-----GFRVVLMYKFEE---ELFL----------RSLQDYKVQSALLVPTLFAF- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 350 kmlglkVNTKRMLGKRDipmnyrmakalvfakvrtslgLDNCHAFFSSASPLSQDVSEFFLS-LDIP-IGEIYGMSECSG 427
Cdd:cd17642 289 ------FAKSTLVDKYD---------------------LSNLHEIASGGAPLSKEVGEAVAKrFKLPgIRQGYGLTETTS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 428 PHTVSNKSVYRVLSCGKVLSGC----------KNMLYNQNkegvGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDI 497
Cdd:cd17642 342 AILITPEGDDKPGAVGKVVPFFyakvvdldtgKTLGPNER----GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDI 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 569000640 498 GRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKEKiPIISHAMLVG 547
Cdd:cd17642 418 AYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQH-PKIFDAGVAG 465
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
39-547 |
3.45e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 127.41 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 39 HGPGHETPMTIPELfqesaERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEwVVTA 118
Cdd:PRK06188 9 HSGATYGHLLVSAL-----KRYPDRPALVLGDT----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE-VLMA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 119 LGTILAGGLC-VGIYATNSAEACQYVIQQANVSILIVENDQQLQKILLIPpDKMETVKAIvqyklplmESMANLYSWNDF 197
Cdd:PRK06188 79 IGAAQLAGLRrTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALL-ARVPSLKHV--------LTLGPVPDGVDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 198 MELGNDIPNIQLDRVILSQKAnqcAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsgKQNTivSYL---PLS 274
Cdd:PRK06188 150 LAAAAKFGPAPLVAAALPPDI---AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-----PADP--RFLmctPLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 275 HIAAqltdiwipikigalTFFAqPDALRGTLVYTLQEVKPtlfmgvpriwEKMQDTIKENvaRSSrlrkkafawAKMLgl 354
Cdd:PRK06188 220 HAGG--------------AFFL-PTLLRGGTVIVLAKFDP----------AEVLRAIEEQ--RIT---------ATFL-- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 355 kVNTkrmlgkrdipMNYRMakaLVFAKVRT----SLGLdnchaFFSSASPLSQD-VSEfflSLDI--PI-GEIYGMSECS 426
Cdd:PRK06188 262 -VPT----------MIYAL---LDHPDLRTrdlsSLET-----VYYGASPMSPVrLAE---AIERfgPIfAQYYGQTEAP 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 427 GPHTVSNK------SVYRVLSCGKVLSGCKNMLYNQNKEGV-----GEVCMWGRHVFMGYLNKEEATLEALdENGWLHSG 495
Cdd:PRK06188 320 MVITYLRKrdhdpdDPKRLTSCGRPTPGLRVALLDEDGREVaqgevGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTG 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 569000640 496 DIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKEKiPIISHAMLVG 547
Cdd:PRK06188 399 DVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVEDVLAEH-PAVAQVAVIG 448
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
75-547 |
4.16e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 126.51 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLI-KLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILI 153
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 154 VENDQQ------LQKILLIPPDKMETVKAIVQYKLplmesmanlyswNDFMELGNDIPNIqldrvilsqkanqcavILYT 227
Cdd:PRK06839 106 VEKTFQnmalsmQKVSYVQRVISITSLKEIEDRKI------------DNFVEKNESASFI----------------ICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 228 SGTTGTPKGVLLSHDNITWTAgaMSQEMEINRVSgkQNTIVSYLPLSHIaaqltdiwipikiGALTFFAQPDALRGTLVY 307
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNA--LNNTFAIDLTM--HDRSIVLLPLFHI-------------GGIGLFAFPTLFAGGVII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 308 T------------LQEVKPTLFMGVPRIWEKMQDTIKenvarssrlrkkafawakmlglkvntkrmlgkrdipmnyrmak 375
Cdd:PRK06839 221 VprkfeptkalsmIEKHKVTVVMGVPTIHQALINCSK------------------------------------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 376 alvfakvRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYR--VLSCGKVLSGCKNML 453
Cdd:PRK06839 258 -------FETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 YNQNKE-----GVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIP 528
Cdd:PRK06839 331 IDENKNkvevgEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLE 408
|
490
....*....|....*....
gi 569000640 529 IETLVkEKIPIISHAMLVG 547
Cdd:PRK06839 409 VEQVI-NKLSDVYEVAVVG 426
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-530 |
4.26e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 122.40 E-value: 4.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 78 TFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVend 157
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 158 qqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgnDIpniqldrvilsqkanqcAVILYTSGTTGTPKGV 237
Cdd:cd05934 82 ---------------------------------------------DP-----------------ASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 238 LLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIAAQLTDIwipikIGALtffaqpdaLRGTLVYTLQEVKPTLF 317
Cdd:cd05934 100 VITHANLTFAGYYSARRFGLGE----DDVYLTVLPLFHINAQAVSV-----LAAL--------SVGATLVLLPRFSASRF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 318 mgvpriWekmqdtikenvarsSRLRKKAFAWAKMLGLkvntkrmlgkrdiPMNYRMAKAlvfAKVRTSlglDNCHAFFSS 397
Cdd:cd05934 163 ------W--------------SDVRRYGATVTNYLGA-------------MLSYLLAQP---PSPDDR---AHRLRAAYG 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 398 ASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYN-QNKE----GVGEVCM-----W 467
Cdd:cd05934 204 APNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDdDGQElpagEPGELVIrglrgW 283
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000640 468 GRhvFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIE 530
Cdd:cd05934 284 GF--FKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVE 342
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
218-566 |
1.01e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 123.32 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 218 ANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFaq 297
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 298 pdalrgtlvytLQEVKPTlfmgvpriwekmqdtikenvARSSRLRKKAFAWakmlglkvntkrMLGKrdIPMNYRMAKAL 377
Cdd:PRK06087 260 -----------LDIFTPD--------------------ACLALLEQQRCTC------------MLGA--TPFIYDLLNLL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 378 VFAKVR-TSLGLdnchaFFSSASPLSQDVSEFFLSLDIPIGEIYGMSEcSGPHTVSN--KSVYRVLSC-GKVLSGCKNML 453
Cdd:PRK06087 295 EKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTE-SSPHAVVNldDPLSRFMHTdGYAAAGVEIKV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 YNQNKEGV-----GEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIP 528
Cdd:PRK06087 369 VDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSRE 447
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 569000640 529 IETLVKeKIPIISHAMLVGDKAKFL----CMLLTLKDRHQNL 566
Cdd:PRK06087 448 VEDILL-QHPKIHDACVVAMPDERLgersCAYVVLKAPHHSL 488
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
222-547 |
2.67e-28 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 117.06 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIAaqltdiwipikiGALTFFAQpdAL 301
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTE----DDNWLCALPLFHIS------------GLSILMRS--VI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 RGTLVYTLQEVKPtlfmgvpriwEKMQDTIKEN-VARSSrlrkkafAWAKMLglkvntKRMLGKRDIPMNYRMAKALvfa 380
Cdd:cd05912 142 YGMTVYLVDKFDA----------EQVLHLINSGkVTIIS-------VVPTML------QRLLEILGEGYPNNLRCIL--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 381 kvrtsLGldnchaffssASPLSQDVSEFFLSLDIPIGEIYGMSE-CSGPHTVSNK-SVYRVLSCGKVLSGC--KNMLYNQ 456
Cdd:cd05912 196 -----LG----------GGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEdALNKIGSAGKPLFPVelKIEDDGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 457 NKEGVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKEk 536
Cdd:cd05912 261 PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEEVLLS- 337
|
330
....*....|.
gi 569000640 537 IPIISHAMLVG 547
Cdd:cd05912 338 HPAIKEAGVVG 348
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-530 |
2.87e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 116.04 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSqemeINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDAL 301
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLA----LNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 RGTLVYT-----LQEVKPTLFMGVPRiwekmqdtikenvarssrlrkkafAWAKMLGLKVNtkrmlgkRDIpmnyrmaKA 376
Cdd:cd05944 81 RNPGLFDnfwklVERYRITSLSTVPT------------------------VYAALLQVPVN-------ADI-------SS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 377 LVFAkvrtslgldnchafFSSASPLSQDV-SEFFLSLDIPIGEIYGMSECSGPHTVSNKS-VYRVLSCG----------K 444
Cdd:cd05944 123 LRFA--------------MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDgPKRPGSVGlrlpyarvriK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 445 VLSGCKNMLYNQNKEGVGEVCMWGRHVFMGYLNKEEAtLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENV 524
Cdd:cd05944 189 VLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLDADGYLFITGRAKD-LIIRGGHNI 266
|
....*.
gi 569000640 525 SPIPIE 530
Cdd:cd05944 267 DPALIE 272
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-542 |
5.52e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 117.73 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 78 TFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEND 157
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 158 qqLQKILLIPPDKMETVKAIVQYKL---PLMESMANLYSWNDFMELGNdiPNIQLDRVilsqKANQCAVILYTSGTTGTP 234
Cdd:cd12119 107 --FLPLLEAIAPRLPTVEHVVVMTDdaaMPEPAGVGVLAYEELLAAES--PEYDWPDF----DENTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 235 KGVLLSHDNItwTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAqltdiW-IPIK---IGALTFFAQPDALRGTLVYTLQ 310
Cdd:cd12119 179 KGVVYSHRSL--VLHAMAALLTDGLGLSESDVVLPVVPMFHVNA-----WgLPYAaamVGAKLVLPGPYLDPASLAELIE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 311 EVKPTLFMGVPRIWekmqdtikenvarssrlrkkafawakmLGLkvntkrmlgkrdipMNYRMAKALVFAKVRTSL--Gl 388
Cdd:cd12119 252 REGVTFAAGVPTVW---------------------------QGL--------------LDHLEANGRDLSSLRRVVigG- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 389 dnchaffsSASPLSqdVSEFFLSLDIPIGEIYGMSECSG-------PHTVSNKSV-----YRVLScGKVLSGCKnmLYNQ 456
Cdd:cd12119 290 --------SAVPRS--LIEAFEERGVRVIHAWGMTETSPlgtvarpPSEHSNLSEdeqlaLRAKQ-GRPVPGVE--LRIV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 457 NKEG---------VGEVCMWGRHVFMGYLNKEEATlEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPI 527
Cdd:cd12119 357 DDDGrelpwdgkaVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSV 434
|
490
....*....|....*
gi 569000640 528 PIETLvkekipIISH 542
Cdd:cd12119 435 ELENA------IMAH 443
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
47-547 |
1.36e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 117.02 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 47 MTIPELFQESAERFSAYPALaSKNGKkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFN-----SVEWVVTALGT 121
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPAL-DFFGA---TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNcpqhiVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 122 I------------LAG-----GLCVGIYATNSAEACQYVIQQAN----VSILIVENDQQLQKILLIPPdkmetVKAIVQY 180
Cdd:PRK05605 108 VvvehnplytaheLEHpfedhGARVAIVWDKVAPTVERLRRTTPletiVSVNMIAAMPLLQRLALRLP-----IPALRKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 181 KLPLMESMANLYSWNDFME--LGNDIPNIQLDRVilsqKANQCAVILYTSGTTGTPKGVLLSHDNITwtAGAMSQEMEIN 258
Cdd:PRK05605 183 RAALTGPAPGTVPWETLVDaaIGGDGSDVSHPRP----TPDDVALILYTSGTTGKPKGAQLTHRNLF--ANAAQGKAWVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 259 RVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGA-LTFFAQPDAlrgTLVytLQEVK---PTLFMGVPRIWEKMQDTIKEn 334
Cdd:PRK05605 257 GLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGeLVLLPAPDI---DLI--LDAMKkhpPTWLPGVPPLYEKIAEAAEE- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 335 varssrlrkkafawakmlglkvntkrmlgkRDIPMNyrmakalvfaKVRTSlgldnchafFSSASPLSQDVSEFFLSLdi 414
Cdd:PRK05605 331 ------------------------------RGVDLS----------GVRNA---------FSGAMALPVSTVELWEKL-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 415 pIG----EIYGMSECSgPHTVSN--KSVYRVLSCGKVLSGCKNMLYNQNKEGV-------GEVCMWGRHVFMGYLNKEEA 481
Cdd:PRK05605 360 -TGgllvEGYGLTETS-PIIVGNpmSDDRRPGYVGVPFPDTEVRIVDPEDPDEtmpdgeeGELLVRGPQVFKGYWNRPEE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000640 482 TLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKEkIPIISHAMLVG 547
Cdd:PRK05605 438 TAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLRE-HPGVEDAAVVG 500
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
45-561 |
3.54e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 115.09 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 45 TPMTiPELF-QESAERFSAYPALAskNGKKWdtLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTIL 123
Cdd:cd12118 2 VPLT-PLSFlERAAAVYPDRTSIV--YGDRR--YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 124 AGGLCVGIYATNSAEACQYVIQQANVSILIVenDQQLQkillippdkmetvkaivqyklplmesmanlysWNDFMELGND 203
Cdd:cd12118 77 AGAVLNALNTRLDAEEIAFILRHSEAKVLFV--DREFE--------------------------------YEDLLAEGDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 204 IPNIQldrvilsQKANQCAVIL--YTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsgKQNTIvsYL---PLSHiAA 278
Cdd:cd12118 123 DFEWI-------PPADEWDPIAlnYTSGTTGRPKGVVYHHRGAYLNALANILEWEM-----KQHPV--YLwtlPMFH-CN 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 279 QLTDIWIPIKIGALTFFaqpdaLR---GTLVYTL-QEVKPTLFMGVPriwekmqdTIKENVARSSRLRKKAFAWakmlgl 354
Cdd:cd12118 188 GWCFPWTVAAVGGTNVC-----LRkvdAKAIYDLiEKHKVTHFCGAP--------TVLNMLANAPPSDARPLPH------ 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 355 KVNTkrMLGKRDIPmnyrmakALVFAKVrTSLGLDNCHAffssasplsqdvsefflsldipigeiYGMSECSGPHTV--- 431
Cdd:cd12118 249 RVHV--MTAGAPPP-------AAVLAKM-EELGFDVTHV--------------------------YGLTETYGPATVcaw 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 432 -------SNKSVYRVlscgKVLSGCKNMLYNQ--------------NKEGVGEVCMWGRHVFMGYLNKEEATLEALdENG 490
Cdd:cd12118 293 kpewdelPTEERARL----KARQGVRYVGLEEvdvldpetmkpvprDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGG 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000640 491 WLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETlVKEKIPIISHAMLVGDKAKFL----CMLLTLKD 561
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEG-VLYKHPAVLEAAVVARPDEKWgevpCAFVELKE 440
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
51-547 |
4.98e-27 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 114.88 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:TIGR03098 4 HLLEDAAARLPDATALVHHD----RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSILiVENDQQLQKILLIPPDKMETVKAIV---QYKLPLMESMANLYSWNDFMELGNDIPni 207
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLL-VTSSERLDLLHPALPGCHDLRTLIIvgdPAHASEGHPGEEPASWPKLLALGDADP-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 208 qLDRVILSQkanqCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIAA--QLTDIWI 285
Cdd:TIGR03098 157 -PHPVIDSD----MAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENR----PDDRLLAVLPLSFDYGfnQLTTAFY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 286 pikIGA----LTFFAQPDALRgtlvyTLQEVKPTLFMGVPRIWEKM-QDTIKENVARSsrLRKKAfawakmlglkvNTkr 360
Cdd:TIGR03098 228 ---VGAtvvlHDYLLPRDVLK-----ALEKHGITGLAAVPPLWAQLaQLDWPESAAPS--LRYLT-----------NS-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 361 mlgkrdipmNYRMAKALVfAKVRTSLgldnchaffssasPLSQdvseFFLsldipigeIYGMSEcsgphtvSNKSVY--- 437
Cdd:TIGR03098 285 ---------GGAMPRATL-SRLRSFL-------------PNAR----LFL--------MYGLTE-------AFRSTYlpp 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 -----RVLSCGKVLSGCKNMLYNQNKE-----GVGEVCMWGRHVFMGYLNKEEATLEALDEN----GWLH-------SGD 496
Cdd:TIGR03098 323 eevdrRPDSIGKAIPNAEVLVLREDGSecapgEEGELVHRGALVAMGYWNDPEKTAERFRPLppfpGELHlpelavwSGD 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 569000640 497 IGRLDSHDFLYITGRiKEILITAGGENVSPIPIETlVKEKIPIISHAMLVG 547
Cdd:TIGR03098 403 TVRRDEEGFLYFVGR-RDEMIKTSGYRVSPTEVEE-VAYATGLVAEAVAFG 451
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
48-533 |
2.95e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 113.05 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASkNGKkwdTLTFSQYYEMCRKAAKSLI-KLGLQRFQCVGILGFNSVEWVVTALGTILAGG 126
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHS-FGK---TITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 127 LCVGIYATNSAEACQYVIQQANVSILIVEND--QQLQKILLIPPDKMETV-----------KAIVQYKLPLMESMANLYS 193
Cdd:PRK08751 102 TVVNVNPLYTPRELKHQLIDSGASVLVVIDNfgTTVQQVIADTPVKQVITtglgdmlgfpkAALVNFVVKYVKKLVPEYR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 194 WN------DFMELG--NDIPNIQLDrvilsqkANQCAVILYTSGTTGTPKGVLLSHDNITwtaGAMSQEMEINRVSGK-- 263
Cdd:PRK08751 182 INgairfrEALALGrkHSMPTLQIE-------PDDIAFLQYTGGTTGVAKGAMLTHRNLV---ANMQQAHQWLAGTGKle 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 264 --QNTIVSYLPLSHIAAQLTDIWIPIKIGALT-FFAQPDALRGtLVYTLQEVKPTLFMGVPRIWEKMQDTikenvarsSR 340
Cdd:PRK08751 252 egCEVVITALPLYHIFALTANGLVFMKIGGCNhLISNPRDMPG-FVKELKKTRFTAFTGVNTLFNGLLNT--------PG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 341 LRKKAFAWAKM-LGLKVNTKRMLGKRdipmnyrmakalvFAKVrTSLGLDNCHAFfSSASPLS----QDVSEFFLSLDIP 415
Cdd:PRK08751 323 FDQIDFSSLKMtLGGGMAVQRSVAER-------------WKQV-TGLTLVEAYGL-TETSPAAcinpLTLKEYNGSIGLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 416 IgeiygmsecsgPHTVS--NKSVYRVLSCGKVlsgcknmlynqnkegvGEVCMWGRHVFMGYLNKEEATLEALDENGWLH 493
Cdd:PRK08751 388 I-----------PSTDAciKDDAGTVLAIGEI----------------GELCIKGPQVMKGYWKRPEETAKVMDADGWLH 440
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 569000640 494 SGDIGRLDSHDFLYITGRIKEILITAGGeNVSPIPIETLV 533
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
76-547 |
5.59e-26 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 110.55 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQAnvsilive 155
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 ndqqLQKILLIPpdkmetvkaivqyklplmesmaNLYSWNDFMELGNDIpniqldrvilsqkanqcAVILYTSGTTGTPK 235
Cdd:cd05903 73 ----KAKVFVVP----------------------ERFRQFDPAAMPDAV-----------------ALLLFTSGTTGEPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 236 GVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQP-DALRGTLVytLQEVKP 314
Cdd:cd05903 110 GVMHSHNTLSASIRQYAERLGL----GPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPDKALAL--MREHGV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 315 TLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKmlglkvntkrmlgkrdIPMNyrmakalVFAKVRTSLGldnchAF 394
Cdd:cd05903 184 TFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGAT----------------VPRS-------LARRAAELLG-----AK 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 395 FSSAsplsqdvsefflsldipigeiYGMSECsgPHTVSN----KSVYRVLSCGKVLSGCKNMLYNQNKEGV-----GEVC 465
Cdd:cd05903 236 VCSA---------------------YGSTEC--PGAVTSitpaPEDRRLYTDGRPLPGVEIKVVDDTGATLapgveGELL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 466 MWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKeKIPIISHAML 545
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAAPE-GWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLLL-GHPGVIEAAV 369
|
..
gi 569000640 546 VG 547
Cdd:cd05903 370 VA 371
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
46-530 |
1.17e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 111.59 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 46 PMTIPELFQESAERFSAYPAL-ASKNGKKWD---TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGT 121
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALsFLLDADPLDrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 122 ILAGGLCvgiyATN---SAEACQYVIQQANVSILI-------VENDQQLQKILlippDKMETVKAIVQykLPLMESMANL 191
Cdd:PRK07529 104 EAAGIAN----PINpllEPEQIAELLRAAGAKVLVtlgpfpgTDIWQKVAEVL----AALPELRTVVE--VDLARYLPGP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 192 YSWND-FMELGNDIPNIQLDRVILSQ-----------KANQCAVILYTSGTTGTPKGVLLSHDNIT---WTAGAMSQEme 256
Cdd:PRK07529 174 KRLAVpLIRRKAHARILDFDAELARQpgdrlfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVanaWLGALLLGL-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 257 inrvsGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDALRGTLVYtlqevkptlfmgvPRIWEKMQdtikenva 336
Cdd:PRK07529 252 -----GPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVI-------------ANFWKIVE-------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 337 rssRLRKKAF-----AWAKMLGLKVntkrmlGKRDIpmnyrmakalvfakvrTSLgldncHAFFSSASPLSQDVSEFFLS 411
Cdd:PRK07529 306 ---RYRINFLsgvptVYAALLQVPV------DGHDI----------------SSL-----RYALCGAAPLPVEVFRRFEA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 412 -LDIPIGEIYGMSECSGPHTVSNKS-VYRVLSCGKVLSGCK----------NMLYNQNKEGVGEVCMWGRHVFMGYLNKE 479
Cdd:PRK07529 356 aTGVRIVEGYGLTEATCVSSVNPPDgERRIGSVGLRLPYQRvrvvilddagRYLRDCAVDEVGVLCIAGPNVFSGYLEAA 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 569000640 480 -EATLEAldENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIE 530
Cdd:PRK07529 436 hNKGLWL--EDGWLNTGDLGRIDADGYFWLTGRAKD-LIIRGGHNIDPAAIE 484
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
74-563 |
2.25e-25 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 109.73 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 74 WDTLTFSQYYemcRKAAKSLIKLG--LQRF----QCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQA 147
Cdd:cd05909 1 EDTLGTSLTY---RKLLTGAIALArkLAKMtkegENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 148 NVSILIVeNDQQLQKILLIPPDKMETVKAIVqyklpLMESMANLYSWND--FMELGNDIPNIQLDRVILS--QKANQCAV 223
Cdd:cd05909 78 GIKTVLT-SKQFIEKLKLHHLFDVEYDARIV-----YLEDLRAKISKADkcKAFLAGKFPPKWLLRIFGVapVQPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 224 ILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAqPDALRG 303
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNP----EDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-PNPLDY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 304 -TLVYTLQEVK-------PTLFMGVPRIWEKMQdtikenvarSSRLRkkafawakmlglkvntkrmlgkrdipmnyrmak 375
Cdd:cd05909 227 kKIPELIYDKKatillgtPTFLRGYARAAHPED---------FSSLR--------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 376 aLVFAkvrtslgldnchaffsSASPLSQDVSEFFLSL-DIPIGEIYGMSECSGPHTVSNKSVYRVLSC-GKVLSGCKNML 453
Cdd:cd05909 265 -LVVA----------------GAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQSPNKEGTvGRPLPGMEVKI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 -----YNQNKEGV-GEVCMWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPI 527
Cdd:cd05909 328 vsvetHEEVPIGEgGLLLVRGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLE 405
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 569000640 528 PIETLVKEKIPI--ISHAMLVGDKAK----FLCMLLTLKDRH 563
Cdd:cd05909 406 AIEDILSEILPEdnEVAVVSVPDGRKgekiVLLTTTTDTDPS 447
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
47-533 |
6.42e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 108.53 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 47 MTIPELFQESAERFSAYPALA-SKNGKkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVeAVTGK---AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGIYATNSAEACQYVIQQANVSiLIVENDQQLQKillippdkmetVKAIvqyKLPLM----ESMANLYSWNDFMELG 201
Cdd:PLN02330 105 GVFSGANPTALESEIKKQAEAAGAK-LIVTNDTNYGK-----------VKGL---GLPVIvlgeEKIEGAVNWKELLEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 202 NDIPNIQLDRVILsqKANQCAvILYTSGTTGTPKGVLLSHDNItwTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAaqlt 281
Cdd:PLN02330 170 DRAGDTSDNEEIL--QTDLCA-LPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEMIGQVVTLGLIPFFHIY---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 282 diwipikigaltffaqpdALRGTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVarssrlrkkAFAwakmlglkvntkrm 361
Cdd:PLN02330 241 ------------------GITGICCATLRNKGKVVVMSRFELRTFLNALITQEV---------SFA-------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 362 lgkrdiPMNYRMAKALVFAKVRTSLGLD--NCHAFFSSASPLSQDVSEFFLSL--DIPIGEIYGMSECS-------GP-- 428
Cdd:PLN02330 280 ------PIVPPIILNLVKNPIVEEFDLSklKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHScitlthgDPek 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 429 -HTVSNKSvyrvlSCGKVLSGCKNMLYNQN------KEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLD 501
Cdd:PLN02330 354 gHGIAKKN-----SVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYID 428
|
490 500 510
....*....|....*....|....*....|..
gi 569000640 502 SHDFLYITGRIKEiLITAGGENVSPIPIETLV 533
Cdd:PLN02330 429 DDGDIFIVDRIKE-LIKYKGFQVAPAELEAIL 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
55-549 |
1.65e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 107.37 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 55 ESAERFSAYPALAskNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLcvgIYAT 134
Cdd:PLN02246 31 ERLSEFSDRPCLI--DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV---TTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 135 N----SAEACQyviqQANVS--ILIVENDQQLQKILLIPPDKMETVKAIVQYKlplmESManLYSWNDFMELGNDIP--N 206
Cdd:PLN02246 106 NpfytPAEIAK----QAKASgaKLIITQSCYVDKLKGLAEDDGVTVVTIDDPP----EGC--LHFSELTQADENELPevE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 207 IQLDRVilsqkanqcaVIL-YTSGTTGTPKGVLLSHDN-ITWTAGAMSQEMEiNRVSGKQNTIVSYLPLSHIAAQLTDIW 284
Cdd:PLN02246 176 ISPDDV----------VALpYSSGTTGLPKGVMLTHKGlVTSVAQQVDGENP-NLYFHSDDVILCVLPMFHIYSLNSVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 285 IPIKIGAlTFFAQPDALRGTLVYTLQEVKPTLFMGVPRIwekmqdtikenvarssrlrkkAFAWAKmlglkvntKRMLGK 364
Cdd:PLN02246 245 CGLRVGA-AILIMPKFEIGALLELIQRHKVTIAPFVPPI---------------------VLAIAK--------SPVVEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 365 RDIpmnyrmakalvfAKVRTSLgldnchaffSSASPLSQDVSEFFLSlDIP---IGEIYGMSEcSGPHTVSN----KSVY 437
Cdd:PLN02246 295 YDL------------SSIRMVL---------SGAAPLGKELEDAFRA-KLPnavLGQGYGMTE-AGPVLAMClafaKEPF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 RVLS--CGKVL-----------SGCkNMLYNQNkegvGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHD 504
Cdd:PLN02246 352 PVKSgsCGTVVrnaelkivdpeTGA-SLPRNQP----GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDD 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 569000640 505 FLYITGRIKEIlITAGGENVSPIPIETLVKEKiPIISHAMLVGDK 549
Cdd:PLN02246 427 ELFIVDRLKEL-IKYKGFQVAPAELEALLISH-PSIADAAVVPMK 469
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
71-547 |
1.24e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 101.19 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 71 GKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVE--WVVTALGTIlaGGLCVGIYATNSAEACQYVIQQAN 148
Cdd:PRK03640 25 EKKV---TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEmiLVIHALQQL--GAVAVLLNTRLSREELLWQLDDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 149 VSILIVENDQQlqkillippDKMETVKAIvqyklplmesmanlySWNDFMELGNDIPNIQ----LDRVilsqkanqcAVI 224
Cdd:PRK03640 100 VKCLITDDDFE---------AKLIPGISV---------------KFAELMNGPKEEAEIQeefdLDEV---------ATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 225 LYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIaaqltdiwipikiGALTffaqpdALRGT 304
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLT----EDDCWLAAVPIFHI-------------SGLS------ILMRS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 305 LVYtlqevkptlfmGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLglkvntKRMLGKrdipmnyrmakalvfakvrt 384
Cdd:PRK03640 204 VIY-----------GMRVVLVEKFDAEKINKLLQTGGVTIISVVSTML------QRLLER-------------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 385 sLGLDNCHAFFSS----ASPLSQDVSEFFLSLDIPIGEIYGMSE-CSGPHTVSNK-SVYRVLSCGKVLSGC-----KNML 453
Cdd:PRK03640 247 -LGEGTYPSSFRCmllgGGPAPKPLLEQCKEKGIPVYQSYGMTEtASQIVTLSPEdALTKLGSAGKPLFPCelkieKDGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 YNQNKEgVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETlV 533
Cdd:PRK03640 326 VVPPFE-EGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEE-V 401
|
490
....*....|....
gi 569000640 534 KEKIPIISHAMLVG 547
Cdd:PRK03640 402 LLSHPGVAEAGVVG 415
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
76-530 |
1.73e-22 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 101.34 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:COG0365 39 TLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDQ-----------QLQKILlippDKMETVKAIVQYKLPLME-SMANLYSWNDFMELGNDipniQLDRVILsqKANQCAV 223
Cdd:COG0365 119 DGGlrggkvidlkeKVDEAL----EELPSLEHVIVVGRTGADvPMEGDLDWDELLAAASA----EFEPEPT--DADDPLF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 224 ILYTSGTTGTPKGVLLSHdniTWTAGAMSQEME----INR------------VSGKQNTIVSylPLSHIAAQLT-Diwip 286
Cdd:COG0365 189 ILYTSGTTGKPKGVVHTH---GGYLVHAATTAKyvldLKPgdvfwctadigwATGHSYIVYG--PLLNGATVVLyE---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 287 ikiGALTFfaqPDAlrGTLVYTLQEVKPTLFMGVPRIWekmqdtikenvaRSsrLRKKAFAWAKmlglkvntkrmlgKRD 366
Cdd:COG0365 260 ---GRPDF---PDP--GRLWELIEKYGVTVFFTAPTAI------------RA--LMKAGDEPLK-------------KYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 367 IpmnyrmakalvfakvrTSLgldncHAFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSGpHTVSNksvYRVL----- 440
Cdd:COG0365 305 L----------------SSL-----RLLGSAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGG-IFISN---LPGLpvkpg 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 441 SCGKVLSGCKNMLYNQN----KEG-VGEVC-------MwgrhvFMGYLNKEEATLEAL--DENGWLHSGDIGRLDSHDFL 506
Cdd:COG0365 360 SMGKPVPGYDVAVVDEDgnpvPPGeEGELVikgpwpgM-----FRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYF 434
|
490 500
....*....|....*....|....
gi 569000640 507 YITGRIKEILITAgGENVSPIPIE 530
Cdd:COG0365 435 WILGRSDDVINVS-GHRIGTAEIE 457
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-547 |
3.48e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 98.12 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 224 ILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEinrvSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQP--DAL 301
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG----LTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsfDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 rgTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKkafawakmlGLkvntkrmlgkrdipmnyrMAKALVfak 381
Cdd:cd05917 83 --AVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRT---------GI------------------MAGAPC--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 382 vrtslgldnchaffssASPLSQDVSEFFLSLDIPIGeiYGMSECSgP---HTVSNKSVY-RVLSCGKVL----------S 447
Cdd:cd05917 131 ----------------PPELMKRVIEVMNMKDVTIA--YGMTETS-PvstQTRTDDSIEkRVNTVGRIMphteakivdpE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 448 GCKNMLYNQnkegVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPI 527
Cdd:cd05917 192 GGIVPPVGV----PGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPR 266
|
330 340
....*....|....*....|
gi 569000640 528 PIETLVkEKIPIISHAMLVG 547
Cdd:cd05917 267 EIEEFL-HTHPKVSDVQVVG 285
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
224-547 |
1.35e-21 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 96.03 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 224 ILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvSGKQNTIVSylPLSHIAAQLTDIWIPIKIGALTF----FAQPD 299
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT--EDDRYLIIN--PFFHTFGYKAGIVACLLTGATVVpvavFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 300 ALRgtlvyTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKafawakmlglkvntkrMLGKRDIPMNY--RMAKAL 377
Cdd:cd17638 81 ILE-----AIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAA----------------VTGAATVPVELvrRMRSEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 378 VFAKVRTSLGLDNCHaffssasplsqdvsefflsldipigeIYGMSECS-GPHTVSNksvyrvlSCGKVLSGcknmlYNQ 456
Cdd:cd17638 140 GFETVLTAYGLTEAG--------------------------VATMCRPGdDAETVAT-------TCGRACPG-----FEV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 457 NKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILItAGGENVSPIPIETLVKEk 536
Cdd:cd17638 182 RIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAE- 259
|
330
....*....|.
gi 569000640 537 IPIISHAMLVG 547
Cdd:cd17638 260 HPGVAQVAVIG 270
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
49-533 |
1.90e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 97.91 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 49 IPELFQESAERFSAYPALaSKNGKkwdTLTFSQYYEMCRKAAKSLIKL-GLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAF-SNLGK---TLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGIYATNSAEACQYVIQQANVSILIVEND--QQLQKIL---------------LIPPDKMETVKAIVQY--KLPLMESM 188
Cdd:PRK05677 102 VVNTNPLYTAREMEHQFNDSGAKALVCLANmaHLAEKVLpktgvkhvivtevadMLPPLKRLLINAVVKHvkKMVPAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 189 ANLYSWNDFMELGNDIPNIQLDrvilsQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQnTIV 268
Cdd:PRK05677 182 PQAVKFNDALAKGAGQPVTEAN-----PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCE-ILI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 269 SYLPLSHIAAQLTDIWIPIKIGALT-FFAQPDALRGtLVYTLQEVKPTLFMGVpriwekmqDTIKENVARSSRLRKKAFA 347
Cdd:PRK05677 256 APLPLYHIYAFTFHCMAMMLIGNHNiLISNPRDLPA-MVKELGKWKFSGFVGL--------NTLFVALCNNEAFRKLDFS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 348 wakmlGLKVNtkrmlgkrdipmnyrmakalvfakvrtslgldnchafFSSASPLSQDVSEFFLSLD-IPIGEIYGMSECS 426
Cdd:PRK05677 327 -----ALKLT-------------------------------------LSGGMALQLATAERWKEVTgCAICEGYGMTETS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 427 GPHTVSNKSVYRVLSCGKVLSG--CKnMLYNQNKE----GVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRL 500
Cdd:PRK05677 365 PVVSVNPSQAIQVGTIGIPVPStlCK-VIDDDGNElplgEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALI 443
|
490 500 510
....*....|....*....|....*....|...
gi 569000640 501 DSHDFLYITGRIKEILITAGGeNVSPIPIETLV 533
Cdd:PRK05677 444 QEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
70-557 |
2.85e-21 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 97.50 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 70 NGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGI---YATNSAE--ACQYVI 144
Cdd:cd05921 19 GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQDlaKLKHLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 145 QQANVSILIVENDQQLQKILlippdkmetvKAIVQYKLPLMESMANLYSWN--DFMELGNDIPNIQLDRVILSQKANQCA 222
Cdd:cd05921 99 ELLKPGLVFAQDAAPFARAL----------AAIFPLGTPLVVSRNAVAGRGaiSFAELAATPPTAAVDAAFAAVGPDTVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 223 VILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMeiNRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGAlTFF---AQPD 299
Cdd:cd05921 169 KFLFTSGSTGLPKAVINTQRMLCANQAMLEQTY--PFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGG-TLYiddGKPM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 300 ALR-GTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVArssrLRKKAFawakmlglkvntkrmlgkrdipmnyrmakalv 378
Cdd:cd05921 246 PGGfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFF-------------------------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 379 fakvrtslglDNCHAFFSSASPLSQDVSEfflSLD----------IPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSG 448
Cdd:cd05921 290 ----------KRLKLMFYAGAGLSQDVWD---RLQalavatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 449 CKNMLYNQNkeGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRL-DSHDF---LYITGRIKEILITAGGENV 524
Cdd:cd05921 357 TELKLVPSG--GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLaDPDDPakgLVFDGRVAEDFKLASGTWV 434
|
490 500 510
....*....|....*....|....*....|....
gi 569000640 525 SPIPIET-LVKEKIPIISHAMLVGDKAKFLCMLL 557
Cdd:cd05921 435 SVGPLRArAVAACAPLVHDAVVAGEDRAEVGALV 468
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
43-542 |
3.11e-21 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 97.35 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 43 HETPMTIPELFQESAERFS-AYPALASKNGKKwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVgILGFNSVEWVVTAL-G 120
Cdd:cd05906 6 EGAPRTLLELLLRAAERGPtKGITYIDADGSE-EFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFwA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 121 TILAGGLCV-----GIYATNSAEACQ--YVIQQANVSILIVEND--QQLQKILLIPPDKMETVKAIvqyklPLMESMANL 191
Cdd:cd05906 84 CVLAGFVPApltvpPTYDEPNARLRKlrHIWQLLGSPVVLTDAElvAEFAGLETLSGLPGIRVLSI-----EELLDTAAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 192 YSWndfmelgndiPNIQLDRVilsqkanqcAVILYTSGTTGTPKGVLLSHDNITwtagAMSQEMEINRVSGKQNTIVSYL 271
Cdd:cd05906 159 HDL----------PQSRPDDL---------ALLMLTSGSTGFPKAVPLTHRNIL----ARSAGKIQHNGLTPQDVFLNWV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 272 PLSHIAAqLTDIWI-PIKIGALTFFAQPDALrgtlvytLQEvkPTLFMgvpriwekmqDTIKEnvarssrlRKKAFAWAk 350
Cdd:cd05906 216 PLDHVGG-LVELHLrAVYLGCQQVHVPTEEI-------LAD--PLRWL----------DLIDR--------YRVTITWA- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 351 mlglkvntkrmlgkrdiPmNYRMAKALVFAKVRT--SLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIG-------EIYG 421
Cdd:cd05906 267 -----------------P-NFAFALLNDLLEEIEdgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 422 MSE-CSG----------PHTVSNKSVyrvlSCGKVLSGCKNMLYNQNKEG-----VGEVCMWGRHVFMGYLNKEEATLEA 485
Cdd:cd05906 329 MTEtCSGviysrsfptyDHSQALEFV----SLGRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEA 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 486 LDENGWLHSGDIGRLDsHDFLYITGRIKEILITaGGENVSPIPIETLVkEKIPIISH 542
Cdd:cd05906 405 FTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIV-NGVNYYSHEIEAAV-EEVPGVEP 458
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
213-541 |
3.37e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 96.79 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 213 ILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSH----IAAQLTDIWIPIK 288
Cdd:cd05908 100 VLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK----TKDRILSWMPLTHdmglIAFHLAPLIAGMN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 289 igaltffaqpdalrgtlvytlQEVKPT-LFMGVPRIWEKMQDTIKENVARS----SRLRKKAFAWAKMLGLKVNTKRMLG 363
Cdd:cd05908 176 ---------------------QYLMPTrLFIRRPILWLKKASEHKATIVSSpnfgYKYFLKTLKPEKANDWDLSSIRMIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 364 KRDIPMNYRMakalvfakvrtslgldnCHAFFSSASPLSQDVSEfflsldipIGEIYGMSECS--------GPHTV---- 431
Cdd:cd05908 235 NGAEPIDYEL-----------------CHEFLDHMSKYGLKRNA--------ILPVYGLAEASvgaslpkaQSPFKtitl 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 432 ----------------SNKSVYRVLSCGKVLSGCKNMLYNQNKEG-----VGEVCMWGRHVFMGYLNKEEATLEALDENG 490
Cdd:cd05908 290 grrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFTDDG 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 569000640 491 WLHSGDIGRLDSHDfLYITGRIKEILITaGGENVSPIPIETLVKEKIPIIS 541
Cdd:cd05908 370 WLKTGDLGFIRNGR-LVITGREKDIIFV-NGQNVYPHDIERIAEELEGVEL 418
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
77-535 |
3.86e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 97.03 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILI--- 153
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcld 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 154 --------VENDQQLQKILLIP-----PDKMETVKAIVQYK----LPLMESMANLYSWNDFMELGNDIPNIQLDrvilsq 216
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVIVTRiadflPFPKNLLYPFVQKKqsnlVVKVSESETIHLWNSVEKEVNTGVEVPCD------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 217 KANQCAVILYTSGTTGTPKGVLLSHDNITwTAGAMSQEMEINRVSGKQnTIVSYLPLSHIAAQLTDIWIPIKIGALTFFA 296
Cdd:PRK06710 204 PENDLALLQYTGGTTGFPKGVMLTHKNLV-SNTLMGVQWLYNCKEGEE-VVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 297 qPDALRGTLVYTLQEVKPTLFMGVPRIWEKMqdtikenvarssrlrkkafawakmlglkvntkrmlgkrdipMNYRMAKA 376
Cdd:PRK06710 282 -PKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-----------------------------------------LNSPLLKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 377 LVFAKVRtslgldnchAFFSSASPLSQDVSEFFLSLDI-PIGEIYGMSEcSGPHTVSN------------------KSVY 437
Cdd:PRK06710 320 YDISSIR---------ACISGSAPLPVEVQEKFETVTGgKLVEGYGLTE-SSPVTHSNflwekrvpgsigvpwpdtEAMI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 RVLSCGKVLSGCKnmlynqnkegVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEiLI 517
Cdd:PRK06710 390 MSLETGEALPPGE----------IGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKD-MI 457
|
490
....*....|....*...
gi 569000640 518 TAGGENVSPIPIETLVKE 535
Cdd:PRK06710 458 VASGFNVYPREVEEVLYE 475
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
223-535 |
3.01e-20 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 91.95 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 223 VILYTSGTTGTPKGVLLSHDNItwtagaMSQEMEINRVSGKQNTIVSY--LPLSHIAAqLTDIWIPIKIGALTF----FA 296
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNL------IAANLQLIHAMGLTEADVYLnmLPLFHIAG-LNLALATFHAGGANVvmekFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 297 QPDALRgtlvyTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKkafawakMLGLkvntkrmlgkrDIPMNYRMAKA 376
Cdd:cd17637 77 PAEALE-----LIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-------VLGL-----------DAPETIQRFEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 377 lvfakvrtslgldNCHAFFSSAsplsqdvsefflsldipigeiYGMSECSGPHTVSnKSVYRVLSCGKVLSGCKNMLYNQ 456
Cdd:cd17637 134 -------------TTGATFWSL---------------------YGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 457 NKEGV-----GEVCMWGRHVFMGYLNKEEATLEALDeNGWLHSGDIGRLDSHDFLYITGRI--KEiLITAGGENVSPIPI 529
Cdd:cd17637 179 NDRPVpagetGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKE-LIKPGGENVYPAEV 256
|
....*.
gi 569000640 530 ETLVKE 535
Cdd:cd17637 257 EKVILE 262
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
71-550 |
5.88e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 93.46 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 71 GKKWDTLTFSQYYEMCRKAAKSLIKLGLQRfQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEA---CQYVIQQA 147
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVGKPG-DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 148 NVSILI--VENDQQLQKILLIPPDKMETVKAIVQyklPLMESMANlySWNDFMELGNDIpniqldrvilsqkanqcAVIL 225
Cdd:cd05931 98 GPRVVLttAAALAAVRAFAASRPAAGTPRLLVVD---LLPDTSAA--DWPPPSPDPDDI-----------------AYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 226 YTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSgkqnTIVSYLPLSHiaaqltDIWIpikIGALTffaQPDALRGTL 305
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD----VVVSWLPLYH------DMGL---IGGLL---TPLYSGGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 306 VYTlqevKPTLFMGVPRIWEKMqdtIKENVARSSrlrkkA---FAW---------AKMLGLKVNTKRMLGK-----RDIP 368
Cdd:cd05931 220 VLM----SPAAFLRRPLRWLRL---ISRYRATIS-----AapnFAYdlcvrrvrdEDLEGLDLSSWRVALNgaepvRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 369 MNyRMAKAlvFAKVrtslGLDnCHAFFSSasplsqdvsefflsldipigeiYGMSEC----------SGPHTVS------ 432
Cdd:cd05931 288 LR-RFAEA--FAPF----GFR-PEAFRPS----------------------YGLAEAtlfvsggppgTGPVVLRvdrdal 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 433 ----------NKSVYRVLSCGKVLSGCKNMLYNQNKE------GVGEVCMWGRHVFMGYLNKEEAT------LEALDENG 490
Cdd:cd05931 338 agravavaadDPAARELVSCGRPLPDQEVRIVDPETGrelpdgEVGEIWVRGPSVASGYWGRPEATaetfgaLAATDEGG 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000640 491 WLHSGDIGRLdsHD-FLYITGRIKEILITAgGENVSPIPIETLVKEkipiiSHAMLVGDKA 550
Cdd:cd05931 418 WLRTGDLGFL--HDgELYITGRLKDLIIVR-GRNHYPQDIEATAEE-----AHPALRPGCV 470
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
70-547 |
8.19e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 92.56 E-value: 8.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 70 NGKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANV 149
Cdd:PRK09088 19 LGRRW---TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 150 SILIveNDQQLQKILLIPpdkmetvkaivqyklplmESMANLYSWNDFMELGnDIPNIQLDRVILsqkanqcavILYTSG 229
Cdd:PRK09088 96 RLLL--GDDAVAAGRTDV------------------EDLAAFIASADALEPA-DTPSIPPERVSL---------ILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 230 TTGTPKGVLLSHDNITWTAGAMSqemeinrVSGKQNTIVSYL---PLSHIaaqltdiwipikIGALTffaqpdalrgtlv 306
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAHNFG-------VLGRVDAHSSFLcdaPMFHI------------IGLIT------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 307 ytlqEVKPTLFMGvpriwekmqdtikenvarSSRLRKKAFAWAKMLGlkvntkrMLGKRDIPMNY-----RMAKALvfak 381
Cdd:PRK09088 194 ----SVRPVLAVG------------------GSILVSNGFEPKRTLG-------RLGDPALGITHyfcvpQMAQAF---- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 382 vRTSLGLD-----NCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSgphTVSNKSV------YRVLSCGKVLSGCK 450
Cdd:PRK09088 241 -RAQPGFDaaalrHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAG---TVFGMSVdcdvirAKAGAAGIPTPTVQ 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 451 NMLYNQNKEGV-----GEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVS 525
Cdd:PRK09088 317 TRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVY 395
|
490 500
....*....|....*....|..
gi 569000640 526 PIPIETLVKEKiPIISHAMLVG 547
Cdd:PRK09088 396 PAEIEAVLADH-PGIRECAVVG 416
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
226-547 |
2.04e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 91.64 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 226 YTSGTTGTPKGVLLSHDNITW---------TAGAMSQEMEInrvsgkqntIVSylPLSHIAA--QLTDIwipiKIGALTF 294
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFvitnhladlMPGTTEQDASL---------VVA--PLSHGAGihQLCQV----ARGAATV 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 295 FAQPDALRGTLVYTL-QEVKPTLFMGVPRIWEKMqdTIKENVAR--SSRLRKKAFAWAKMLglKVNTKRMLGKrdipmny 371
Cdd:PRK07470 235 LLPSERFDPAEVWALvERHRVTNLFTVPTILKML--VEHPAVDRydHSSLRYVIYAGAPMY--RADQKRALAK------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 372 rMAKALVfakvrtslgldnchaffssasplsqdvsefflsldipigEIYGMSECSG-----P---HTVSNKSVYRVLSCG 443
Cdd:PRK07470 304 -LGKVLV---------------------------------------QYFGLGEVTGnitvlPpalHDAEDGPDARIGTCG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 444 KVLSGCKnmLYNQNKEG-------VGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEIL 516
Cdd:PRK07470 344 FERTGME--VQIQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY 420
|
330 340 350
....*....|....*....|....*....|....
gi 569000640 517 ITaGGENVSPIPIEtlvkEKI---PIISHAMLVG 547
Cdd:PRK07470 421 IS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
227-530 |
3.81e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.83 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 227 TSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGkqnTIVSYLPLSHiaaqltdiwipiKIGALTFFAQPDALRGTLV 306
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETD---VMVSWLPLFH------------DMGMVGFLTVPMYFGAELV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 307 YtlqeVKPTLFMGVPRIWEKMQDTIKENVARSSrlrkkAFAWAkMLGlkvntkRMLGKRDIPMNYRMAkALVFAkvrtsl 386
Cdd:PRK07768 225 K----VTPMDFLRDPLLWAELISKYRGTMTAAP-----NFAYA-LLA------RRLRRQAKPGAFDLS-SLRFA------ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 387 gldnchafFSSASPLSQDVSEFFLSLDIPIG-------EIYGMSE---------CSGPHTV----------------SNK 434
Cdd:PRK07768 282 --------LNGAEPIDPADVEDLLDAGARFGlrpeailPAYGMAEatlavsfspCGAGLVVdevdadllaalrravpATK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 435 SVYRVLSC-GKVLSGCKNMLYNQNKE-----GVGEVCMWGRHVFMGYLNkEEATLEALDENGWLHSGDIGRLDSHDFLYI 508
Cdd:PRK07768 354 GNTRRLATlGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVV 432
|
330 340
....*....|....*....|..
gi 569000640 509 TGRIKEILITaGGENVSPIPIE 530
Cdd:PRK07768 433 CGRVKDVIIM-AGRNIYPTDIE 453
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
48-555 |
4.34e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 91.52 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKNGKkwdTLTfsqYYEMCRKAA--KSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADSTGG---ELS---YGKALTGALalARLLKRELKDEENVGILLPPSVAGALANLALLLAG 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGIYATNSAEACQYVIQQANVSILI--------------VENDQQLQKILLIP-----PDKMETVKAIVQYK-LPLm 185
Cdd:PRK08633 690 KVPVNLNYTASEAALKSAIEQAQIKTVItsrkfleklknkgfDLELPENVKVIYLEdlkakISKVDKLTALLAARlLPA- 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 186 esmanlyswndFMELGNDIPNIQLDRVilsqkanqcAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQN 265
Cdd:PRK08633 769 -----------RLLKRLYGPTFKPDDT---------ATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRN----DD 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 266 TIVSYLPLSHiAAQLT-DIWIPIKIGALTFFaQPDALRGtlvytlqevkptlfmgvpriwEKMQDTIKENvaRSSRLrkk 344
Cdd:PRK08633 825 VILSSLPFFH-SFGLTvTLWLPLLEGIKVVY-HPDPTDA---------------------LGIAKLVAKH--RATIL--- 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 345 aFAWAKMLGLKVNTKRmlgkrdipmnyrmAKALVFAKVRTSLgldnchaffSSASPLSQDVSEFF-LSLDIPIGEIYGMS 423
Cdd:PRK08633 877 -LGTPTFLRLYLRNKK-------------LHPLMFASLRLVV---------AGAEKLKPEVADAFeEKFGIRILEGYGAT 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 424 ECSGPHTVSNKSVYRVLScgKVLSGCKN-----------------MLYNQNKEGV-GEVCMWGRHVFMGYLNKEEATLEA 485
Cdd:PRK08633 934 ETSPVASVNLPDVLAADF--KRQTGSKEgsvgmplpgvavrivdpETFEELPPGEdGLILIGGPQVMKGYLGDPEKTAEV 1011
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000640 486 L---DENGWLHSGDIGRLDSHDFLYITGRIK---EIlitaGGENVSPIPIEtlvkEKIpiisHAMLVGDKAKFLCM 555
Cdd:PRK08633 1012 IkdiDGIGWYVTGDKGHLDEDGFLTITDRYSrfaKI----GGEMVPLGAVE----EEL----AKALGGEEVVFAVT 1075
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
222-547 |
8.95e-19 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 87.39 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsGKQNTIVSyLPLSHIAAqLTDIWIPIKIGALTFFAQPDAL 301
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFG---GGDSWLLS-LPLYHVGG-LAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 rgtLVYTLQEVKPTLFMGVPRIWEKMQDtikenvarssrlRKKAFAWAKMLGlkvntkrmlgkrdipmnyrmakalvfak 381
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPTQLQRLLD------------SGQGPAALKSLR---------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 382 vrtslgldnchAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQnkegv 461
Cdd:cd17630 115 -----------AVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 462 GEVCMWGRHVFMGYLNKEEAtlEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVkEKIPIIS 541
Cdd:cd17630 179 GEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVR 254
|
....*.
gi 569000640 542 HAMLVG 547
Cdd:cd17630 255 DAFVVG 260
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-548 |
8.97e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 89.04 E-value: 8.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIAAqLTDIWIPIKIGALTFFAQPDAL 301
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 RGTLVYTLQEVKPTLFMGVPRIWEkMQDTIKenvarssrlrkkafaWAKMlglKVNTKRMLGKrdipMNYRMAKALVfak 381
Cdd:cd05922 195 DDAFWEDLREHGATGLAGVPSTYA-MLTRLG---------------FDPA---KLPSLRYLTQ----AGGRLPQETI--- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 382 vrtslgldnchAFFSSASPLSQdvsefflsldipIGEIYGMSECSG------PHTVSNKSVyrvlSCGKVLSGCKNMLYN 455
Cdd:cd05922 249 -----------ARLRELLPGAQ------------VYVMYGQTEATRrmtylpPERILEKPG----SIGLAIPGGEFEILD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 456 Q------NKEgVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAgGENVSPIPI 529
Cdd:cd05922 302 DdgtptpPGE-PGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEI 379
|
330
....*....|....*....
gi 569000640 530 ETLVKEkIPIISHAMLVGD 548
Cdd:cd05922 380 EAAARS-IGLIIEAAAVGL 397
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
77-547 |
1.94e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 88.70 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVen 156
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 DQQLQkillippdkmetvkaivQYKLPLMESMANLYSWNDFMELGNDIPNIQLD----------RVILSQKANQC----- 221
Cdd:PLN02860 111 DETCS-----------------SWYEELQNDRLPSLMWQVFLESPSSSVFIFLNsflttemlkqRALGTTELDYAwapdd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 -AVILYTSGTTGTPKGVLLSHDNITwtagamSQEMEINRVSGKQNTIVsYL---PLSHIAAqLTDIWIPIKIGALTFFAq 297
Cdd:PLN02860 174 aVLICFTSGTTGRPKGVTISHSALI------VQSLAKIAIVGYGEDDV-YLhtaPLCHIGG-LSSALAMLMVGACHVLL- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 298 PDALRGTLVYTLQEVKPTLFMGVPRIwekMQDTIKenVARSSRLRKKAFAWAKMLGlkvntkrmlGKRDIPMNYRMAKAL 377
Cdd:PLN02860 245 PKFDAKAALQAIKQHNVTSMITVPAM---MADLIS--LTRKSMTWKVFPSVRKILN---------GGGSLSSRLLPDAKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 378 VF--AKVRTSLGL-DNChaffSSASplsqdvsefFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSC-GKVLSGCKNML 453
Cdd:PLN02860 311 LFpnAKLFSAYGMtEAC----SSLT---------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCvGKPAPHVELKI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 YNQNKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEIlITAGGENVSPIPIETLV 533
Cdd:PLN02860 378 GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDR-IKTGGENVYPEEVEAVL 456
|
490
....*....|....
gi 569000640 534 KEKiPIISHAMLVG 547
Cdd:PLN02860 457 SQH-PGVASVVVVG 469
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
48-547 |
2.30e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.20 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPAL--ASKNGKKwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALifESSGGVV-RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGIYATNSAEACQYVIQQANVSILIVE-------------NDQQLQKILLIPPDKMETVKAIvqyklplmesmanly 192
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSaqfypmyrqiqqeDATPLRHICLTRVALPADDGVS--------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 193 swnDFMELGNDIPNIQLDRVILSqkANQCAVILYTSGTTGTPKGVLLSHDNITWtAGAMSQEMEINRvsgKQNTIVSYLP 272
Cdd:PRK08008 152 ---SFTQLKAQQPATLCYAPPLS--TDDTAEILFTSGTTSRPKGVVITHYNLRF-AGYYSAWQCALR---DDDVYLTVMP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 273 LSHIAAQLTDIWIPIKIGAL----------TFFAQPDALRGTLVYTLQEVKPTLFMGVPRIWEkmqdtikenvaRSSRLR 342
Cdd:PRK08008 223 AFHIDCQCTAAMAAFSAGATfvllekysarAFWGQVCKYRATITECIPMMIRTLMVQPPSAND-----------RQHCLR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 343 KKAFawakMLGLKVNTKRMLGKRdipmnyrmakalvFaKVRtslgldnchaFFSSasplsqdvsefflsldipigeiYGM 422
Cdd:PRK08008 292 EVMF----YLNLSDQEKDAFEER-------------F-GVR----------LLTS----------------------YGM 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 423 SEC-SGPHTVSNKSVYRVLSCGKV-LSGCKNMLYNQNKE----GVGEVCMWG---RHVFMGYLNKEEATLEALDENGWLH 493
Cdd:PRK08008 322 TETiVGIIGDRPGDKRRWPSIGRPgFCYEAEIRDDHNRPlpagEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLH 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 569000640 494 SGDIGRLDSHDFLYITGRiKEILITAGGENVSPIPIETLVkEKIPIISHAMLVG 547
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELENII-ATHPKIQDIVVVG 453
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
76-547 |
2.69e-18 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 87.52 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgnDIpniqldrvilsqkanqcAVILYTSGTTGTPK 235
Cdd:cd05919 90 AD---------------------------------------------DI-----------------AYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 236 GVLLSHDNITWTAGAMSQEMeinrVSGKQNTIVSYLPLSHIAAQL-TDIWIPIKIGA--LTFFAQPDALRgtLVYTLQEV 312
Cdd:cd05919 108 GVMHAHRDPLLFADAMAREA----LGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGAsaVLNPGWPTAER--VLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 313 KPTLFMGVPRIWEKMqdtikenvarssrLRKKAFAWAKMLGLKVntkrmlgkrdipmnyrmakalvfakvrtslgldnch 392
Cdd:cd05919 182 RPTVLYGVPTFYANL-------------LDSCAGSPDALRSLRL------------------------------------ 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 393 aFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSgpHT-VSNK-SVYRVLSCGKVLSGCKNMLYNQnkEG-------VG 462
Cdd:cd05919 213 -CVSAGEALPRGLGERWMEhFGGPILDGIGATEVG--HIfLSNRpGAWRLGSTGRPVPGYEIRLVDE--EGhtippgeEG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 463 EVCMWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKEkIPIISH 542
Cdd:cd05919 288 DLLVRGPSAAVGYWNNPEKSRATFNG-GWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQ-HPAVAE 364
|
....*
gi 569000640 543 AMLVG 547
Cdd:cd05919 365 AAVVA 369
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
49-531 |
5.15e-18 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 87.04 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 49 IPELFQESAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLC 128
Cdd:cd05959 6 ATLVDLNLNEGRGDKTAFIDDAG----SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 129 VGIYATNSAEACQYVIQQANVSILIVEndQQLQKILLIPPDKMETVKAIVQYKLPLMESMAnlyswndFMELGNDIPNIQ 208
Cdd:cd05959 82 VPVNTLLTPDDYAYYLEDSRARVVVVS--GELAPVLAAALTKSEHTLVVLIVSGGAGPEAG-------ALLLAELVAAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 209 LDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQemeiNRVSGKQNTIVsylpLShiAAQL-------T 281
Cdd:cd05959 153 EQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYAR----NVLGIREDDVC----FS--AAKLffayglgN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 282 DIWIPIKIGALTF----FAQPDAlrgtLVYTLQEVKPTLFMGVPRIWEKMqdtikenvarssrlrkkafawakmlgLKVN 357
Cdd:cd05959 223 SLTFPLSVGATTVlmpeRPTPAA----VFKRIRRYRPTVFFGVPTLYAAM--------------------------LAAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 358 TkrmLGKRDipmnyrmakalvFAKVRTSLgldnchaffSSASPLSQDVSEFF---LSLDIPIGeiYGMSE-----CSG-P 428
Cdd:cd05959 273 N---LPSRD------------LSSLRLCV---------SAGEALPAEVGERWkarFGLDILDG--IGSTEmlhifLSNrP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 429 HTVsnksvyRVLSCGKVLSGCKNMLYNQNKE-----GVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSH 503
Cdd:cd05959 327 GRV------RYGTTGKPVPGYEVELRDEDGGdvadgEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDD 399
|
490 500
....*....|....*....|....*...
gi 569000640 504 DFLYITGRIKEiLITAGGENVSPIPIET 531
Cdd:cd05959 400 GFYTYAGRADD-MLKVSGIWVSPFEVES 426
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
43-524 |
5.56e-18 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 87.51 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 43 HETPMTIPELFQESAERFSAYPALASKNGK----------------KWDTLTFSQYYE-MCRKAAKSLIKLGLQRFQCVG 105
Cdd:cd17632 18 RRPGLRLAQIIATVMTGYADRPALGQRATElvtdpatgrttlrllpRFETITYAELWErVGAVAAAHDPEQPVRPGDFVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 106 ILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENDQ------------QLQKILLIP--PDKM 171
Cdd:cd17632 98 VLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHldlaveavleggTPPRLVVFDhrPEVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 172 ETVKAIVQYKLPLMESMANLYSWNDFMELGNDIPNIQLDRVilSQKANQCAVILYTSGTTGTPKGVLLSHDNITwTAGAM 251
Cdd:cd17632 178 AHRAALESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRP--EPDDDPLALLIYTSGSTGTPKGAMYTERLVA-TFWLK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 252 SQEMEINRVSGKQNtiVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDAlrGTLVYTLQEVKPTLFMGVPRIWEKMQDTI 331
Cdd:cd17632 255 VSSIQDIRPPASIT--LNFMPMSHIAGRISLYGTLARGGTAYFAAASDM--STLFDDLALVRPTELFLVPRVCDMLFQRY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 332 KENVARSSRLRKKAFAWAKMLGLKVNtKRMLGKRdipmnYRMAkalvfakvrtslgldnchafFSSASPLSQDVSEFFLS 411
Cdd:cd17632 331 QAELDRRSVAGADAETLAERVKAELR-ERVLGGR-----LLAA--------------------VCGSAPLSAEMKAFMES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 412 -LDIPIGEIYGMSEcSGPHTVSNKSV------YRVLSCGKVlsgckNMLYNQNKEGVGEVCMWGRHVFMGYLNKEEATLE 484
Cdd:cd17632 385 lLDLDLHDGYGSTE-AGAVILDGVIVrppvldYKLVDVPEL-----GYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 569000640 485 ALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENV 524
Cdd:cd17632 459 VFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFV 498
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
77-547 |
2.09e-17 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 85.25 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEN 156
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 DQQLQKILLIPPDKMETVKAIVQYKLPlmesmanlYSWNDFMElgndipniqlDRvilSQKANQCAVILYTSGTTGTPKG 236
Cdd:cd05923 109 DAQVMDAIFQSGVRVLALSDLVGLGEP--------ESAGPLIE----------DP---PREPEQPAFVFYTSGTTGLPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 237 VLLSHDNITWTAGAMSQEMEiNRVsGKQNTIVSYLPLSHIaaqltdiwipikIGALTFFAQPDALRGTLVytlqevkptl 316
Cdd:cd05923 168 AVIPQRAAESRVLFMSTQAG-LRH-GRHNVVLGLMPLYHV------------IGFFAVLVAALALDGTYV---------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 317 fmgVPRiwekmqdtikenvarssrlrkkAFAWAKMLGLkVNTKRMLGKRDIPMNYrmaKALVFAKVRTSLGLDNC-HAFF 395
Cdd:cd05923 224 ---VVE----------------------EFDPADALKL-IEQERVTSLFATPTHL---DALAAAAEFAGLKLSSLrHVTF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 396 SSAS---PLSQDVSEFflsLDIPIGEIYGMSEC--------SGPHTVSNKSVYRVLSCGKVLSGCKNMLYNqNKEGVGEV 464
Cdd:cd05923 275 AGATmpdAVLERVNQH---LPGEKVNIYGTTEAmnslymrdARTGTEMRPGFFSEVRIVRIGGSPDEALAN-GEEGELIV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 465 CMWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKEKiPIISHAM 544
Cdd:cd05923 351 AAAADAAFTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVV 427
|
...
gi 569000640 545 LVG 547
Cdd:cd05923 428 VIG 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
222-531 |
2.64e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 84.66 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNIT-----------WTAgamsqemeinrvsgkQNTIVSYLPLSHIAAQLTDIWIPIKIG 290
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAadldalaeawqWTA---------------DDVLVHGLPLFHVHGLVLGVLGPLRIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 291 altffaqpdalrGTLVYTlqeVKP-------------TLFMGVPRIWEKMQDtiKENVARssrlrkkAFAWAKMLglkvn 357
Cdd:PRK07787 196 ------------NRFVHT---GRPtpeayaqalseggTLYFGVPTVWSRIAA--DPEAAR-------ALRGARLL----- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 358 tkrMLGKRDIPmnyrmakALVFAKVRTSLGLdnchaffssasplsqdvsefflsldiPIGEIYGMSEcsgphTVSNKSVY 437
Cdd:PRK07787 247 ---VSGSAALP-------VPVFDRLAALTGH--------------------------RPVERYGMTE-----TLITLSTR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 -----RVLSCGKVLSGCKNMLYNQNK-------EGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDF 505
Cdd:PRK07787 286 adgerRPGWVGLPLAGVETRLVDEDGgpvphdgETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGM 365
|
330 340
....*....|....*....|....*.
gi 569000640 506 LYITGRIKEILITAGGENVSPIPIET 531
Cdd:PRK07787 366 HRIVGRESTDLIKSGGYRIGAGEIET 391
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
222-547 |
1.17e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 82.90 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITwtagamSQEMEINRVSG-KQNTIVSYL--PLSHIAAqLTDIWIPIKIGALTFFAQP 298
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLT------GQAMTCLRTNGaDINSDVGFVgvPLFHIAG-IGSMLPGLLLGAPTVIYPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 299 DALR-GTLVYTLQEVKPTLFMGVPRIWekmQDTIKENVARSSRLRKKAFAWAkmlglkvntkrmlgkrdipmnyrmakal 377
Cdd:PRK07786 250 GAFDpGQLLDVLEAEKVTGIFLVPAQW---QAVCAEQQARPRDLALRVLSWG---------------------------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 378 vfAKVRTSLGLDNCHAFFssasPLSQDVSEFflsldipigeiyGMSECSgPHT---VSNKSVYRVLSCGKVLSGCKNMLY 454
Cdd:PRK07786 299 --AAPASDTLLRQMAATF----PEAQILAAF------------GQTEMS-PVTcmlLGEDAIRKLGSVGKVIPTVAARVV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 455 NQNKEGV-----GEVCMWGRHVFMGYLNKEEATLEALDeNGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPI 529
Cdd:PRK07786 360 DENMNDVpvgevGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEV 437
|
330
....*....|....*...
gi 569000640 530 ETLVKEKiPIISHAMLVG 547
Cdd:PRK07786 438 ENVLASH-PDIVEVAVIG 454
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
222-535 |
1.31e-16 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 81.15 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNItWTAGAMSQEMEINRVSGkqNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDAL 301
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTF-FAVPDILQKEGLNWVVG--DVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 RgTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRMLGKRDIPMNYRMAKALVFAK 381
Cdd:cd17635 81 K-SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 382 VRTSLGLDNCHAffssasplsqdVSEFFLSLDIPIGEIYGMSECSGphtvsnksvyrvlscgkvlsgcknmlynqnkeGV 461
Cdd:cd17635 160 LPTDDDSIEINA-----------VGRPYPGVDVYLAATDGIAGPSA--------------------------------SF 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000640 462 GEVCMWGRHVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEIlITAGGENVSPIPIETLVKE 535
Cdd:cd17635 197 GTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFLFITGRSSES-INCGGVKIAPDEVERIAEG 268
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
57-547 |
2.28e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 81.86 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 57 AERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNS 136
Cdd:PRK06145 12 ARRTPDRAALVYRD----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 137 AEACQYVIQQANVSILIVenDQQLQ-------KILLIPPDKMETVKAIVQYKLPLMESMANLYSwnDFMELgndipniql 209
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLV--DEEFDaivaletPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPT--DLVRL--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 210 drvilsqkanqcaviLYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvsgKQNTIVSYLPLSHIAAqltdiwipIKI 289
Cdd:PRK06145 155 ---------------MYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLT----ASERLLVVGPLYHVGA--------FDL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 290 GALTFFAQPDALRgtlvyTLQEVKPtlfmgvpriwekmqDTIKENVARSsRLRKKAFAwakmlglKVNTKRMLGkrdIPM 369
Cdd:PRK06145 208 PGIAVLWVGGTLR-----IHREFDP--------------EAVLAAIERH-RLTCAWMA-------PVMLSRVLT---VPD 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 370 NYRMAkalvFAKVRTSLGldnchafFSSASPLSQ--DVSEFFLSLDIPIGeiYGMSE-CSGPHTV-SNKSVYRVLSCGKV 445
Cdd:PRK06145 258 RDRFD----LDSLAWCIG-------GGEKTPESRirDFTRVFTRARYIDA--YGLTEtCSGDTLMeAGREIEKIGSTGRA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 446 L--------SGCKNMLY-NQNkegvGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEIL 516
Cdd:PRK06145 325 LahveiriaDGAGRWLPpNMK----GEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI 399
|
490 500 510
....*....|....*....|....*....|.
gi 569000640 517 ITaGGENVSPIPIETLVKEkIPIISHAMLVG 547
Cdd:PRK06145 400 IS-GGENIASSEVERVIYE-LPEVAEAAVIG 428
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
39-258 |
2.51e-16 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 82.98 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 39 HGPGHETP--MTIPELFQESAERFSAYPALASKNGkkwdTLTfsqYYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVE 113
Cdd:COG1020 466 NATAAPYPadATLHELFEAQAARTPDAVAVVFGDQ----SLT---YAELNARAnrlAHHLRALGVGPGDLVGVCLERSLE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 114 WVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENDqqlqkillippdkmetvkaiVQYKLPlmesmanlys 193
Cdd:COG1020 539 MVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSA--------------------LAARLP---------- 588
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000640 194 wndfmelGNDIPNIQLDRVILSQ----------KANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEIN 258
Cdd:COG1020 589 -------ELGVPVLALDALALAAepatnppvpvTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLG 656
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
56-547 |
3.37e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.51 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 56 SAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVeWVVTALGTilAGGLCVGIYATN 135
Cdd:PRK07788 58 AARRAPDRAALIDERG----TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHR-GFVLALYA--AGKVGARIILLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 136 ---SAEACQYVIQQANVSILIVenDQQLQKILLIPPDKMETVKAIVQYKLPLMESMANLYSWNDFMELGNDIPniqldrv 212
Cdd:PRK07788 131 tgfSGPQLAEVAAREGVKALVY--DDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAP------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 213 iLSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMsqemeINRVSGKQN-TIVSYLPLSHIA--AQLTDIWipiki 289
Cdd:PRK07788 202 -LPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGL-----LSRVPFRAGeTTLLPAPMFHATgwAHLTLAM----- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 290 galtffaqpdALRGTLVytlqevkptlfmgVPRIWeKMQDTIkENVARssrlrKKAFAwakMLGLKVNTKRMLgkrDIPm 369
Cdd:PRK07788 271 ----------ALGSTVV-------------LRRRF-DPEATL-EDIAK-----HKATA---LVVVPVMLSRIL---DLG- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 370 nyrmakalvfAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLdipIGEI----YGMSECS------------GPHTVsn 433
Cdd:PRK07788 314 ----------PEVLAKYDTSSLKIIFVSGSALSPELATRALEA---FGPVlynlYGSTEVAfatiatpedlaeAPGTV-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 434 ksvyrvlscGKVLSGCKNMLY--NQNKEGVGEVcmwGR------HVFMGYLN---KEEAtlealdeNGWLHSGDIGRLDS 502
Cdd:PRK07788 379 ---------GRPPKGVTVKILdeNGNEVPRGVV---GRifvgngFPFEGYTDgrdKQII-------DGLLSSGDVGYFDE 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 569000640 503 HDFLYITGRIKEiLITAGGENVSPIPIETLVKEKiPIISHAMLVG 547
Cdd:PRK07788 440 DGLLFVDGRDDD-MIVSGGENVFPAEVEDLLAGH-PDVVEAAVIG 482
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
19-514 |
8.21e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 80.69 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 19 AVPRL-WSTHCDGEVLLRlSKHGPGhETPMTIPELFQESAERFSAYPALASKNGK-KWDTLTFSQYYEMCRKAAKSLIKL 96
Cdd:PRK08180 12 APPAVeVERRADGTIYLR-SAEPLG-DYPRRLTDRLVHWAQEAPDRVFLAERGADgGWRRLTYAEALERVRAIAQALLDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 97 GLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGI---YATNSA--EACQYVIQQANVSILIVENDQQLQK-ILLIPPDK 170
Cdd:PRK08180 90 GLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQdfGKLRHVLELLTPGLVFADDGAAFARaLAAVVPAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 171 METVkaIVQYKLPLMESMAnlyswndFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGA 250
Cdd:PRK08180 170 VEVV--AVRGAVPGRAATP-------FAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 251 MSQ---EMEINRVsgkqnTIVSYLPLSHIAAQLTDIWIPIKIGAlTFF---AQP-DALRGTLVYTLQEVKPTLFMGVPRI 323
Cdd:PRK08180 241 LAQtfpFLAEEPP-----VLVDWLPWNHTFGGNHNLGIVLYNGG-TLYiddGKPtPGGFDETLRNLREISPTVYFNVPKG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 324 WEKMQDTIKENVArssrLRKKAFAWAKMLglkvntkrmlgkrdipmnyrmakalvfakvrtslgldnchaFFSSASpLSQ 403
Cdd:PRK08180 315 WEMLVPALERDAA----LRRRFFSRLKLL-----------------------------------------FYAGAA-LSQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 404 DVSEfflSLD----------IPIGEIYGMSECSGPHTvsnkSVYRVLSC----GKVLSGCKNMLYNQNkeGVGEVCMWGR 469
Cdd:PRK08180 349 DVWD---RLDrvaeatcgerIRMMTGLGMTETAPSAT----FTTGPLSRagniGLPAPGCEVKLVPVG--GKLEVRVKGP 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 569000640 470 HVFMGYLNKEEATLEALDENGWLHSGDIGRL-DSHDF---LYITGRIKE 514
Cdd:PRK08180 420 NVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPADPergLMFDGRIAE 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
76-549 |
1.09e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.89 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIK-LGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 EndqqlqkillipPDKMETVKAIvqyKLPLMeSMANLYSWND-------FMELGNDIPNIQLDRVILSQKAnqcAVILYT 227
Cdd:PLN02574 146 S------------PENVEKLSPL---GVPVI-GVPENYDFDSkriefpkFYELIKEDFDFVPKPVIKQDDV---AAIMYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 228 SGTTGTPKGVLLSHDNITWTAGAMSQ-EMEINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIG-ALTFFAQPDAlrGTL 305
Cdd:PLN02574 207 SGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGsTIVVMRRFDA--SDM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 306 VYTLQEVKPTLFMGVPRIwekmqdtikenvarssrlrkkafawakMLGLKvntkrmlgkrdipmnyRMAKAlVFAKVRTS 385
Cdd:PLN02574 285 VKVIDRFKVTHFPVVPPI---------------------------LMALT----------------KKAKG-VCGEVLKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 386 LGLDNChaffsSASPLS----QDVSEFFLSLDIPIGeiYGMSECS--GPHTVSNKSVYRVLSCG--------KVL---SG 448
Cdd:PLN02574 321 LKQVSC-----GAAPLSgkfiQDFVQTLPHVDFIQG--YGMTESTavGTRGFNTEKLSKYSSVGllapnmqaKVVdwsTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 449 CknMLYNQNKegvGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEIlITAGGENVSPIP 528
Cdd:PLN02574 394 C--LLPPGNC---GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEI-IKYKGFQIAPAD 467
|
490 500
....*....|....*....|..
gi 569000640 529 IETLVKEKIPIISHAML-VGDK 549
Cdd:PLN02574 468 LEAVLISHPEIIDAAVTaVPDK 489
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
394-547 |
5.23e-15 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 76.29 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 394 FFSSASPLSQDVSEFF--LSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQNKEGVGEVCMWGRHV 471
Cdd:cd17633 115 IFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMV 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000640 472 FMGYLNKEEATlealdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKeKIPIISHAMLVG 547
Cdd:cd17633 195 FSGYVRGGFSN-----PDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPGIEEAIVVG 263
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
51-512 |
5.78e-15 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 77.37 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSILIVENDQQlqkillIPPDKMETVkaivqyklpLMESMANLYSWndfmelgndiPNIQLD 210
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQ------PPIAFIGLI---------DLLDEDTIYHE----------ESENLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 211 RVIlsqKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMeinrVSGKQNTIVSYLPLShIAAQLTDIWIPIKIG 290
Cdd:cd17655 132 PVS---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI----YQGEHLRVALFASIS-FDASVTEIFASLLSG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 291 A-LTFFAQPDALRG-TLVYTLQEVKPTLFMGVP---RIWEKMQDTIKENVAR--------SSRLRKKafaWAKMLGLKVN 357
Cdd:cd17655 204 NtLYIVRKETVLDGqALTQYIRQNRITIIDLTPahlKLLDAADDSEGLSLKHlivggealSTELAKK---IIELFGTNPT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 358 TkrmlgkrdipMNyrmakalVFAKVRTSLGldnCHAFFSSASPLSQDvsefflslDIPIGEiygmsecsgphTVSNKSVY 437
Cdd:cd17655 281 I----------TN-------AYGPTETTVD---ASIYQYEPETDQQV--------SVPIGK-----------PLGNTRIY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 RVLSCGKVLSgcknmlynqnkEGV-GEVCMWGRHVFMGYLNKEEATLEALDENGWL------HSGDIGRL--DSH-DFLy 507
Cdd:cd17655 322 ILDQYGRPQP-----------VGVaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWlpDGNiEFL- 389
|
....*
gi 569000640 508 itGRI 512
Cdd:cd17655 390 --GRI 392
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
77-547 |
6.63e-15 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 77.13 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEN 156
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 dqQLQKILLIPpdkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkanqcavilYTSGTTGTPKG 236
Cdd:cd05935 82 --ELDDLALIP----------------------------------------------------------YTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 237 VLLSHDNITWTAgamSQEMEINRVSGkQNTIVSYLPLSHIAAQLTDIWIPIKIGaltffaqpdalrGTLVytlqevkptl 316
Cdd:cd05935 102 CMHTHFSAAANA---LQSAVWTGLTP-SDVILACLPLFHVTGFVGSLNTAVYVG------------GTYV---------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 317 FMGvprIWEkmQDTIKENVARssrlRKKAFAWA--KMLGLKVNTKRmLGKRDipmnyrMAKALVFAkvrtslgldnchaf 394
Cdd:cd05935 156 LMA---RWD--RETALELIEK----YKVTFWTNipTMLVDLLATPE-FKTRD------LSSLKVLT-------------- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 395 fSSASPLSQDVSEFFLSL-DIPIGEIYGMSE-CSGPHTvsNKSVYRVLSC---------GKVLSGCKNMLYNQNKEGvgE 463
Cdd:cd05935 206 -GGGAPMPPAVAEKLLKLtGLRFVEGYGLTEtMSQTHT--NPPLRPKLQClgip*fgvdARVIDIETGRELPPNEVG--E 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 464 VCMWGRHVFMGYLNKEEATLEALDENG---WLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVkEKIPII 540
Cdd:cd05935 281 IVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKR-MINVSGFKVWPAEVEAKL-YKHPAI 358
|
....*..
gi 569000640 541 SHAMLVG 547
Cdd:cd05935 359 *EVCVIS 365
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
197-548 |
1.10e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 77.07 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 197 FMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNtiVSYLPLSHI 276
Cdd:PTZ00342 282 IILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTH--LSYLPISHI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 277 -------AAQLTDIWIPIKIGALTFFAQpdalrgtlvyTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKafawa 349
Cdd:PTZ00342 360 yerviayLSFMLGGTINIWSKDINYFSK----------DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRF----- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 350 kmlglkvNTKRMLGKRDIPMNYRMAKAL-----VFAKVRTSLGlDNCHAFFSSASPLSQDV-SEFFLSLDIPIGEIYGMS 423
Cdd:PTZ00342 425 -------LVKKILSLRKSNNNGGFSKFLegithISSKIKDKVN-PNLEVILNGGGKLSPKIaEELSVLLNVNYYQGYGLT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 424 ECSGPHTVSNKSVYRVLSCGKVLSgcKNMLYN---------QNKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHS 494
Cdd:PTZ00342 497 ETTGPIFVQHADDNNTESIGGPIS--PNTKYKvrtwetykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 569000640 495 GDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKEkIPIISHAMLVGD 548
Cdd:PTZ00342 575 GDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQ-ISFINFCVVYGD 627
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
75-512 |
1.77e-14 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 75.75 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGglcvgiyatnsaeaCQYVIqqanvsiliV 154
Cdd:cd05945 15 RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG--------------HAYVP---------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 ENDQqlqkilliPPDKMETVKAIVQYKLplmesmanlyswndFMELGNDIpniqldrvilsqkanqcAVILYTSGTTGTP 234
Cdd:cd05945 72 DASS--------PAERIREILDAAKPAL--------------LIADGDDN-----------------AYIIFTSGSTGRP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 235 KGVLLSHDNI-TWTAGAMSQEMeinrvSGKQNTIVSYLPLSHIAAqLTDIWIPIKIGALTFFAQPDALR--GTLVYTLQE 311
Cdd:cd05945 113 KGVQISHDNLvSFTNWMLSDFP-----LGPGDVFLNQAPFSFDLS-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 312 VKPTLFMGVPRIWEkMQDTIKE-NVARSSRLRKKAFAwakmlG--LKVNTKRMLGKRdipmnyrmakalvfakvrtslgl 388
Cdd:cd05945 187 HGITVWVSTPSFAA-MCLLSPTfTPESLPSLRHFLFC-----GevLPHKTARALQQR----------------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 389 dnchafFSSAsplsqdvsefflsldiPIGEIYGMSECSGP---HTVSNKSV--YRVLSCGKVLSGCKNMLYNQNKEGV-- 461
Cdd:cd05945 238 ------FPDA----------------RIYNTYGPTEATVAvtyIEVTPEVLdgYDRLPIGYAKPGAKLVILDEDGRPVpp 295
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 462 ---GEVCMWGRHVFMGYLNKEEATLEALDEN---GWLHSGDIGRLDSHDFLYITGRI 512
Cdd:cd05945 296 gekGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRL 352
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
47-530 |
2.34e-14 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 75.95 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 47 MTIPELFQESAERFSAYPaLASKNGKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGG 126
Cdd:PRK06155 21 RTLPAMLARQAERYPDRP-LLVFGGTRW---TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 127 LCVGIYATNSAEACQYVIQQANVSILIVE------------NDQQLQKILLIPPDKMETVKAIVQYkLPLMESMANLysw 194
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEaallaaleaadpGDLPLPAVWLLDAPASVSVPAGWST-APLPPLDAPA--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 195 ndfmelgnDIPNIQldrvilsqkANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLS 274
Cdd:PRK06155 173 --------PAAAVQ---------PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEI----GADDVLYTTLPLF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 275 HIAAQ-------LTDIWIPI--KIGALTFFAQPDALRGTLVYTLQEVKPTLfmgvpriwekmqdtikenVARSSRLRKKA 345
Cdd:PRK06155 232 HTNALnaffqalLAGATYVLepRFSASGFWPAVRRHGATVTYLLGAMVSIL------------------LSQPARESDRA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 346 FAwakmlglkvntkrmlgkrdipmnyrmakalvfakVRTSLGldnchaffsSASPlSQDVSEFFLSLDIPIGEIYGMSEC 425
Cdd:PRK06155 294 HR----------------------------------VRVALG---------PGVP-AALHAAFRERFGVDLLDGYGSTET 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 426 SGPHTVSNKSvYRVLSCGKVLSGCKNMLYNQNKEGV-----GEVCMWGR--HVFM-GYLNKEEATLEALdENGWLHSGDI 497
Cdd:PRK06155 330 NFVIAVTHGS-QRPGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADepFAFAtGYFGMPEKTVEAW-RNLWFHTGDR 407
|
490 500 510
....*....|....*....|....*....|...
gi 569000640 498 GRLDSHDFLYITGRIKEIlITAGGENVSPIPIE 530
Cdd:PRK06155 408 VVRDADGWFRFVDRIKDA-IRRRGENISSFEVE 439
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
222-533 |
4.22e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 75.09 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNI-------TWTAGAMSQEmeinrvsgKQNTIVSYLPLSHIAAqLTdiwipikIGALTF 294
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMlanleqaKAAYGPLLHP--------GKELVVTALPLYHIFA-LT-------VNCLLF 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 295 FAqpdaLRGTlvytlqevkpTLFMGVPRiweKMQDTIKEnvarssrLRKKAFAwaKMLGlkVNT--KRMLGKRDIpmnyr 372
Cdd:PRK08974 273 IE----LGGQ----------NLLITNPR---DIPGFVKE-------LKKYPFT--AITG--VNTlfNALLNNEEF----- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 373 maKALVFAKVRTSLGldnchaffsSASPLSQDVSEFFLSL-DIPIGEIYGMSECS-----GPHT-----------VSNKS 435
Cdd:PRK08974 320 --QELDFSSLKLSVG---------GGMAVQQAVAERWVKLtGQYLLEGYGLTECSplvsvNPYDldyysgsiglpVPSTE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 436 VYRVLSCGKVLSgcknmlynqNKEgVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEI 515
Cdd:PRK08974 389 IKLVDDDGNEVP---------PGE-PGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDM 457
|
330
....*....|....*...
gi 569000640 516 lITAGGENVSPIPIETLV 533
Cdd:PRK08974 458 -ILVSGFNVYPNEIEDVV 474
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
222-530 |
6.69e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 74.15 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSH----IAAQLTD------IWIPI--KI 289
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRL----SPRDATVAVMPLYHghglIAALLATlasggaVLLPArgRF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 290 GALTFFAQPDAlrgtlvytlqeVKPTLFMGVPRIWEKMQDTIKENVARSSRlrkkafawakmlglkvntkrmlgkrdipm 369
Cdd:PRK05852 255 SAHTFWDDIKA-----------VGATWYTAVPTIHQILLERAATEPSGRKP----------------------------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 370 nyrmaKALVFAKvrtslgldnchaffSSASPLSQDVSEF----FLSldiPIGEIYGMSECSgpHTVSNKSVYR------- 438
Cdd:PRK05852 295 -----AALRFIR--------------SCSAPLTAETAQAlqteFAA---PVVCAFGMTEAT--HQVTTTQIEGigqtenp 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 439 VLSCGKVLSGCKNMLYNQNKEG-------VGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGR 511
Cdd:PRK05852 351 VVSTGLVGRSTGAQIRIVGSDGlplpagaVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGR 429
|
330
....*....|....*....
gi 569000640 512 IKEiLITAGGENVSPIPIE 530
Cdd:PRK05852 430 IKE-LINRGGEKISPERVE 447
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
222-533 |
7.10e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 74.47 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGK------QNTIVSYLPLSHIAAqltdiwipikigaltFF 295
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQplmkegQEVMIAPLPLYHIYA---------------FT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 296 AQPDALRGTLVYTLQEVKPTLFMGVpriwekmqdtIKEnvarssrLRKKAFAwaKMLGLkvNTKRMlgkrdIPMNYRMAK 375
Cdd:PRK12492 275 ANCMCMMVSGNHNVLITNPRDIPGF----------IKE-------LGKWRFS--ALLGL--NTLFV-----ALMDHPGFK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 376 ALVFakvrTSLGLDNchaffSSASPLSQDVSEFFLSLD-IPIGEIYGMSECSgPHTVSNK--SVYRVLSCGKVLSGckNM 452
Cdd:PRK12492 329 DLDF----SALKLTN-----SGGTALVKATAERWEQLTgCTIVEGYGLTETS-PVASTNPygELARLGTVGIPVPG--TA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 453 LYNQNKEGV-------GEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGeNVS 525
Cdd:PRK12492 397 LKVIDDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF-NVY 475
|
....*...
gi 569000640 526 PIPIETLV 533
Cdd:PRK12492 476 PNEIEDVV 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-512 |
2.14e-13 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 72.30 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 90 AKSLIKL-GLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVenDQQLQkillipP 168
Cdd:TIGR01733 13 ARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT--DSALA------S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 169 DKMETVKAIVqyklplmesmanLYSWNDFMELGNDIPNIQLDRVilsQKANQCAVILYTSGTTGTPKGVLLSHDNITWTA 248
Cdd:TIGR01733 85 RLAGLVLPVI------------LLDPLELAALDDAPAPPPPDAP---SGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 249 GAMSQEMEINRVSgkqnTIVSYLPLSHIAAqLTDIWIPIKIGALTFFAQPDALRGTLV---YTLQEVKPTLFMGVPRIWE 325
Cdd:TIGR01733 150 AWLARRYGLDPDD----RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDDAAllaALIAEHPVTVLNLTPSLLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 326 KMQDtikENVARSSRLRKKAFA--WAkmlglkvnTKRMLGKrdipmnyrmakalvFAKVRTSLGLDN----------CHA 393
Cdd:TIGR01733 225 LLAA---ALPPALASLRLVILGgeAL--------TPALVDR--------------WRARGPGARLINlygptettvwSTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 394 FFSSASPLSQDVSefflsldIPIGeiygmsecsgpHTVSNKSVYRVLSCGK-VLSGCknmlynqnkegVGEVCMWGRHVF 472
Cdd:TIGR01733 280 TLVDPDDAPRESP-------VPIG-----------RPLANTRLYVLDDDLRpVPVGV-----------VGELYIGGPGVA 330
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 569000640 473 MGYLNKEEATLE--------ALDENGWLHSGDIGRLDSHDFLYITGRI 512
Cdd:TIGR01733 331 RGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
48-533 |
2.41e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 72.75 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKnGKkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICM-GK---AITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGI---YATNSAEacqyviQQANVS----ILIVEN-DQQLQKILLIPPDKMETVKA----------IVQY------KLP 183
Cdd:PRK07059 100 VVNVnplYTPRELE------HQLKDSgaeaIVVLENfATTVQQVLAKTAVKHVVVASmgdllgfkghIVNFvvrrvkKMV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 184 LMESMANLYSWNDFMELGNdipNIQLDRVILSqkANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEME---INRV 260
Cdd:PRK07059 174 PAWSLPGHVRFNDALAEGA---RQTFKPVKLG--PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpafEKKP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 261 SGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALT-FFAQPDALRGtLVYTLQEVKPTLFMGVPRIWEKMqdtikenvarss 339
Cdd:PRK07059 249 RPDQLNFVCALPLYHIFALTVCGLLGMRTGGRNiLIPNPRDIPG-FIKELKKYQVHIFPAVNTLYNAL------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 340 rlrkkafawakmlglkvntkrmlgkrdipMNYRMAKALVFAKVRTSLGldnchaffsSASPLSQDVSEFFLSLD-IPIGE 418
Cdd:PRK07059 316 -----------------------------LNNPDFDKLDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 419 IYGMSECSgPhtvsnksvyrVLSCGKV----LSGCKNM------LYNQNKEG-------VGEVCMWGRHVFMGYLNKEEA 481
Cdd:PRK07059 358 GYGLSETS-P----------VATCNPVdateFSGTIGLplpsteVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDE 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 569000640 482 TLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLV 533
Cdd:PRK07059 427 TAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD-MILVSGFNVYPNEIEEVV 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
51-512 |
4.20e-13 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 71.57 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASKngkkWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:cd17653 1 DAFERIAAAHPDAVAVESL----GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSilivendqqlqkiLLIPPDKmetvkaivqyklplmesmanlyswndfmelGNDIpniqld 210
Cdd:cd17653 77 LDAKLPSARIQAILRTSGAT-------------LLLTTDS------------------------------PDDL------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 211 rvilsqkanqcAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInRVSGKQNTIVSylplshIA--AQLTDIWIPIK 288
Cdd:cd17653 108 -----------AYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDV-GPGSRVAQVLS------IAfdACIGEIFSTLC 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 289 IGALTFFAQPDAlrgTLVYTLQEVkpTLFMGVPRIWEKMQDTikenvarssrlrkkafawakmlglkvntkrmlgkrdip 368
Cdd:cd17653 170 NGGTLVLADPSD---PFAHVARTV--DALMSTPSILSTLSPQ-------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 369 mnyrmakalvfakvrtslGLDNCHAFFSSASPLSQDVSEFFlSLDIPIGEIYGMSECSgpHTVSNKSVY--RVLSCGKVL 446
Cdd:cd17653 207 ------------------DFPNLKTIFLGGEAVPPSLLDRW-SPGRRLYNAYGPTECT--ISSTMTELLpgQPVTIGKPI 265
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 447 SGCKNMLYNQNKEGV-----GEVCMWGRHVFMGYLNKEEAT----LEALDENGWLH--SGDIGRLDSHDFLYITGRI 512
Cdd:cd17653 266 PNSTCYILDADLQPVpegvvGEICISGVQVARGYLGNPALTaskfVPDPFWPGSRMyrTGDYGRWTEDGGLEFLGRE 342
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
77-547 |
6.35e-13 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 70.83 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEn 156
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 dqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkANQCAVILYTSGTTGTPKG 236
Cdd:cd05972 80 -------------------------------------------------------------AEDPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 237 VLLSHdniTWTAGAMSqemeinrvsgkqnTIVSYLPL--SHIAAQLTDI-WIpikIGALTFFAQPdALRG--TLVYTLQE 311
Cdd:cd05972 99 VLHTH---SYPLGHIP-------------TAAYWLGLrpDDIHWNIADPgWA---KGAWSSFFGP-WLLGatVFVYEGPR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 312 VKPtlfmgvpriwEKMQDTIKEnvarssrlrkkafawakmlgLKVNTkrMLGKrdiPMNYRM-AKALVFAKVRTSLgldn 390
Cdd:cd05972 159 FDA----------ERILELLER--------------------YGVTS--FCGP---PTAYRMlIKQDLSSYKFSHL---- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 391 cHAFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSgpHTVSNKSVYRVL--SCGKVLSGCKNMLYNQNKEG-----VG 462
Cdd:cd05972 200 -RLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTETG--LTVGNFPDMPVKpgSMGRPTPGYDVAIIDDDGRElppgeEG 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 463 EVCM-WGRHV-FMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEIlITAGGENVSPIPIE-TLVKEkiPI 539
Cdd:cd05972 277 DIAIkLPPPGlFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDI-IKSSGYRIGPFEVEsALLEH--PA 352
|
....*...
gi 569000640 540 ISHAMLVG 547
Cdd:cd05972 353 VAEAAVVG 360
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
51-245 |
6.47e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 71.08 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDR----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSILIVenDQQLQKILLIPPDKMETVKAIVQYKLPLmesmanlyswndfmelgndiPNIQLD 210
Cdd:cd12117 77 LDPELPAERLAFMLADAGAKVLLT--DRSLAGRAGGLEVAVVIDEALDAGPAGN--------------------PAVPVS 134
|
170 180 190
....*....|....*....|....*....|....*
gi 569000640 211 rvilsqkANQCAVILYTSGTTGTPKGVLLSHDNIT 245
Cdd:cd12117 135 -------PDDLAYVMYTSGSTGRPKGVAVTHRGVV 162
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
222-535 |
1.10e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 70.29 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQ---P 298
Cdd:PRK07514 159 AAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRF----TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPkfdP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 299 DALRGTLVytlqevKPTLFMGVPRIWEKMQDtikenvarSSRLRKKAfawakmlglkvnTKRMlgkrdipmnyRMakalv 378
Cdd:PRK07514 235 DAVLALMP------RATVMMGVPTFYTRLLQ--------EPRLTREA------------AAHM----------RL----- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 379 fakvrtslgldnchaFFSSASPLSQDV-SEFFLSLDIPIGEIYGMSEC----SGPH-------TV----SNKSVyRVLSC 442
Cdd:PRK07514 274 ---------------FISGSAPLLAEThREFQERTGHAILERYGMTETnmntSNPYdgerragTVgfplPGVSL-RVTDP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 443 --GKVLsgcknmlynqnkeGVGEVCMW---GRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILI 517
Cdd:PRK07514 338 etGAEL-------------PPGEIGMIevkGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLII 404
|
330
....*....|....*...
gi 569000640 518 TaGGENVSPIPIETLVKE 535
Cdd:PRK07514 405 S-GGYNVYPKEVEGEIDE 421
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
76-512 |
1.57e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 69.48 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTfsqYYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSIL 152
Cdd:cd05930 12 SLT---YAELDARAnrlARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 153 IVEndqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkANQCAVILYTSGTTG 232
Cdd:cd05930 89 LTD--------------------------------------------------------------PDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 233 TPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSHIAAqLTDIWIPIKIGALTFFAQPDALR--GTLVYTLQ 310
Cdd:cd05930 107 KPKGVMVEHRGLVNLLLWMQEAYPL----TPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEEVRKdpEALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 311 EVKPTLFMGVPRIWEKMQDTIKENVARSSRLrkkafawaKMLGLKVNTKRMLGKrdipmnyrmakalvFAKVRTSLGLDN 390
Cdd:cd05930 182 EEGITVLHLTPSLLRLLLQELELAALPSLRL--------VLVGGEALPPDLVRR--------------WRELLPGARLVN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 391 CH-----AFFSSASPLSQDVSEfflSLDIPIGeiygmsecsgpHTVSNKSVYrvlscgkVLSGcknmlyNQN--KEGV-G 462
Cdd:cd05930 240 LYgpteaTVDATYYRVPPDDEE---DGRVPIG-----------RPIPNTRVY-------VLDE------NLRpvPPGVpG 292
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 463 EVCMWGRHVFMGYLNKEEATLEA-----LDENGWLH-SGDIGRLDSH-DFLYItGRI 512
Cdd:cd05930 293 ELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDgNLEFL-GRI 348
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
87-530 |
2.61e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 69.35 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 87 RKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGI----------YATNSAEAcQYVIQQANVSILIVEN 156
Cdd:PRK07008 50 KQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTInprlfpeqiaYIVNHAED-RYVLFDLTFLPLVDAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 DQQLQK----ILLIPPDKMETVKAIVQYKLPLMESMANLYSWNDFMElgndipniqldrvilsqkaNQCAVILYTSGTTG 232
Cdd:PRK07008 129 APQCPNvkgwVAMTDAAHLPAGSTPLLCYETLVGAQDGDYDWPRFDE-------------------NQASSLCYTSGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 233 TPKGVLLSHDNITWTA--GAMSQEMEINrvsgKQNTIVSYLPLSHIAAqltdiW-IPIK---IGALTFFAQPDaLRGTLV 306
Cdd:PRK07008 190 NPKGALYSHRSTVLHAygAALPDAMGLS----ARDAVLPVVPMFHVNA-----WgLPYSaplTGAKLVLPGPD-LDGKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 307 YTLQEV-KPTLFMGVPRIWEKMQDTIKENVARSSRLRkkafawakmlglkvntkrmlgkrdipmnyrmakalvfakvRTS 385
Cdd:PRK07008 260 YELIEAeRVTFSAGVPTVWLGLLNHMREAGLRFSTLR----------------------------------------RTV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 386 LGldnchaffSSASPLSQdVSEFFLSLDIPIGEIYGMSECSGPHTVS---NKSVYR--------VLSCGKVLSGCKNMLY 454
Cdd:PRK07008 300 IG--------GSACPPAM-IRTFEDEYGVEVIHAWGMTEMSPLGTLCklkWKHSQLpldeqrklLEKQGRVIYGVDMKIV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 455 NQN-KE----GV--GEVCMWGRHVFMGYLNKEEATLealdENGWLHSGDIGRLDSHDFLYITGRIKEIlITAGGENVSPI 527
Cdd:PRK07008 371 GDDgRElpwdGKafGDLQVRGPWVIDRYFRGDASPL----VDGWFPTGDVATIDADGFMQITDRSKDV-IKSGGEWISSI 445
|
...
gi 569000640 528 PIE 530
Cdd:PRK07008 446 DIE 448
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
459-530 |
3.33e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 68.82 E-value: 3.33e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000640 459 EGVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:PRK08162 386 ETIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVE 455
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
211-547 |
4.09e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 68.23 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 211 RVILSQKANQCAVILYTSGTTGTPKGVLLSHdnitwtagamsqemeinRVsgkqntIVSYLPLSHIAAQL----TDI-WI 285
Cdd:cd05971 80 SALVTDGSDDPALIIYTSGTTGPPKGALHAH-----------------RV------LLGHLPGVQFPFNLfprdGDLyWT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 286 PIK---IGALtffaqpdalrgtlvytLQEVKPTLFMGVPRIWEKMQdtikenvarssRLRKKAfAWAKMLGLKVNTKRMl 362
Cdd:cd05971 137 PADwawIGGL----------------LDVLLPSLYFGVPVLAHRMT-----------KFDPKA-ALDLMSRYGVTTAFL- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 363 gkrdIPMNYRMAKALVFAKVRTSLGLdncHAFFSSASPLSQD----VSEFFlslDIPIGEIYGMSECSgpHTVSNKSVY- 437
Cdd:cd05971 188 ----PPTALKMMRQQGEQLKHAQVKL---RAIATGGESLGEEllgwAREQF---GVEVNEFYGQTECN--LVIGNCSALf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 --RVLSCGKVLSGCKNMLYNQNKE-----GVGEVCMW--GRHVFMGYLNKEEATlEALDENGWLHSGDIGRLDSHDFLYI 508
Cdd:cd05971 256 piKPGSMGKPIPGHRVAIVDDNGTplppgEVGEIAVElpDPVAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWY 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 569000640 509 TGRIKEIlITAGGENVSPIPIE-TLVKEkiPIISHAMLVG 547
Cdd:cd05971 335 VGRDDDV-ITSSGYRIGPAEIEeCLLKH--PAVLMAAVVG 371
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
74-559 |
4.24e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 68.69 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 74 WDTLTFSQYYEMCRKAAKSL-IKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSiL 152
Cdd:PRK06334 39 WDEQLGKLSYNQVRKAVIALaTKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVT-H 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 153 IVENDQQLQKILLIPPDKMEtvkaiVQYKLPLMESMANLYSWNDFMELG--NDIPNIQLDRV--ILSQKANQCAVILYTS 228
Cdd:PRK06334 118 VLTSKQLMQHLAQTHGEDAE-----YPFSLIYMEEVRKELSFWEKCRIGiyMSIPFEWLMRWfgVSDKDPEDVAVILFTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 229 GTTGTPKGVLLSHDNITwtagaMSQEMEINRVSGKQNTI-VSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDALRGTLVY 307
Cdd:PRK06334 193 GTEKLPKGVPLTHANLL-----ANQRACLKFFSPKEDDVmMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 308 TLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRkkafawakmlglkvntkrmlgkrdipmnyrmakalvFAKVrtslG 387
Cdd:PRK06334 268 MIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLR------------------------------------FVVI----G 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 388 LDnchAFFSSaspLSQDVSEFFLSLDIPIGeiYGMSECSGPHTVSNKSVYRVLSC-GKVLSGCKNMLYNQNKEG------ 460
Cdd:PRK06334 308 GD---AFKDS---LYQEALKTFPHIQLRQG--YGTTECSPVITINTVNSPKHESCvGMPIRGMDVLIVSEETKVpvssge 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 461 VGEVCMWGRHVFMGYL-NKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKE---- 535
Cdd:PRK06334 380 TGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLEALESILMEgfgq 458
|
490 500
....*....|....*....|....*....
gi 569000640 536 -----KIPIISHAmLVGDKAKfLCMLLTL 559
Cdd:PRK06334 459 naadhAGPLVVCG-LPGEKVR-LCLFTTF 485
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
29-550 |
7.03e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 68.15 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 29 DGEVLLRlSKHGPGhETPMTIPELFQESAERFSAYPALASKNG--KKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGI 106
Cdd:PRK12582 33 DGSIVIK-SRHPLG-PYPRSIPHLLAKWAAEAPDRPWLAQREPghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 107 LGFNSVEWVVTALGTILAGGLCVGI---YATNSAE--ACQYVIQQANVSILIVENDQQLQKILLIPpdKMETVKAIVQYK 181
Cdd:PRK12582 111 LSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAAL--DLLDVTVVHVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 182 LPlmESMANLyswnDFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITwTAGAMSQEMEINRVS 261
Cdd:PRK12582 189 PG--EGIASI----AFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMC-ANIAMQEQLRPREPD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 262 GKQNTIVSYLPLSHIAAQlTDIWIPIKIGALTFFAQPD----ALRGTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVAr 337
Cdd:PRK12582 262 PPPPVSLDWMPWNHTMGG-NANFNGLLWGGGTLYIDDGkplpGMFEETIRNLREISPTVYGNVPAGYAMLAEAMEKDDA- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 338 ssrLRKKAFawaKMLGLkvntkrmlgkrdipMNYRMAKalvfakvrtslgldnchaffssaspLSQDVSEFFLSL----- 412
Cdd:PRK12582 340 ---LRRSFF---KNLRL--------------MAYGGAT-------------------------LSDDLYERMQALavrtt 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 413 --DIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCK-NMLYNQNKEgvgEVCMWGRHVFMGYLNKEEATLEALDEN 489
Cdd:PRK12582 375 ghRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVElKLAPVGDKY---EVRVKGPNVTPGYHKDPELTAAAFDEE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 490 GWLHSGDIGR-LDSHDF---LYITGRIKEILITAGGENVSPIPIET-LVKEKIPIISHAMLVG-DKA 550
Cdd:PRK12582 452 GFYRLGDAARfVDPDDPekgLIFDGRVAEDFKLSTGTWVSVGTLRPdAVAACSPVIHDAVVAGqDRA 518
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-302 |
7.78e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.65 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 52 LFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGI 131
Cdd:PRK12467 517 LIEAQARQHPERPALVFGE----QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 132 YATNSAEACQYVIQQANVSILIveNDQQLQKILLIPPDkmetvkaivqykLPLMESMANLYSWNDFMELGNDIPniqldr 211
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLL--TQSHLLAQLPVPAG------------LRSLCLDEPADLLCGYSGHNPEVA------ 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 212 vilsQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSgkqntivSYLPLSHIAAQL--TDIWIPIKI 289
Cdd:PRK12467 653 ----LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-------SMLMVSTFAFDLgvTELFGALAS 721
|
250
....*....|...
gi 569000640 290 GALTFFAQPDALR 302
Cdd:PRK12467 722 GATLHLLPPDCAR 734
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
75-258 |
1.33e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 66.91 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 ENDQQLQKILLIPpdkmetvkaivqyklplmesmaNLYSWNDFMELGNDIPNIQLDrvilsqkANQCAVILYTSGTTGTP 234
Cdd:cd12114 91 DGPDAQLDVAVFD----------------------VLILDLDALAAPAPPPPVDVA-------PDDLAYVIFTSGSTGTP 141
|
170 180
....*....|....*....|....
gi 569000640 235 KGVLLSHDNITWTAGAMSQEMEIN 258
Cdd:cd12114 142 KGVMISHRAALNTILDINRRFAVG 165
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
461-533 |
4.06e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 65.64 E-value: 4.06e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000640 461 VGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLV 533
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGENISSLEVENVV 472
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
418-547 |
5.31e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 65.19 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 418 EIYGMSECSG-PHTVSNKSVYRVLSCGKvlsGCKNMLYNQNKEGvGEVCMWGR----HV-----FMGYLNkEEATLEALD 487
Cdd:PRK07638 284 EFYGASELSFvTALVDEESERRPNSVGR---PFHNVQVRICNEA-GEEVQKGEigtvYVkspqfFMGYII-GGVLARELN 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 488 ENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKEkIPIISHAMLVG 547
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIESVLHE-HPAVDEIVVIG 416
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
77-533 |
6.91e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 65.04 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEN 156
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 DQQ--LQKIL-LIPPDKME---TVKAIVQYKLPLMESMANLySWNDFMELGNDIPNIqLDRVILSQKANQCAVILYTSGT 230
Cdd:PLN03102 120 SFEplAREVLhLLSSEDSNlnlPVIFIHEIDFPKRPSSEEL-DYECLIQRGEPTPSL-VARMFRIQDEHDPISLNYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 231 TGTPKGVLLSHDN--ITWTAGAMSQEMEINRVsgkqntIVSYLPLSHIAAqltdiWIpikigaltfFAQPDALRGTLVYT 308
Cdd:PLN03102 198 TADPKGVVISHRGayLSTLSAIIGWEMGTCPV------YLWTLPMFHCNG-----WT---------FTWGTAARGGTSVC 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 309 LQEVKptlfmgVPRIWEKMQdtiKENVARSSRLrKKAFAWAkMLGLKVNTKRMLGKRDIPMNYRMAKALVFAKVRtSLGL 388
Cdd:PLN03102 258 MRHVT------APEIYKNIE---MHNVTHMCCV-PTVFNIL-LKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 389 DNCHAffssasplsqdvsefflsldipigeiYGMSECSGP------------------HTVSNKSVYRVLSCGKVLSGCK 450
Cdd:PLN03102 326 QVMHA--------------------------YGLTEATGPvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 451 NMLYNQNKEG--VGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIP 528
Cdd:PLN03102 380 ETQESVPRDGktMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVE 457
|
....*
gi 569000640 529 IETLV 533
Cdd:PLN03102 458 VENVL 462
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
76-245 |
2.17e-10 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 62.88 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDQqlqkillipPDKMETVKAIVQYKLPLMesmanlyswndFMELGNDIPniqldrviLSQKANQCAVILYTSGTTGTPK 235
Cdd:cd17656 93 RHL---------KSKLSFNKSTILLEDPSI-----------SQEDTSNID--------YINNSDDLLYIIYTSGTTGKPK 144
|
170
....*....|
gi 569000640 236 GVLLSHDNIT 245
Cdd:cd17656 145 GVQLEHKNMV 154
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-569 |
2.58e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 62.83 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 78 TFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEND 157
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 158 qqlqkILLIPPDKMETVKAIVQYklPLMESMANLYSwnDFMELGNdiPNIQLDRVIlsqkaNQCAVIL--YTSGTTGTPK 235
Cdd:cd05915 106 -----LLPLVEAIRGELKTVQHF--VVMDEKAPEGY--LAYEEAL--GEEADPVRV-----PERAACGmaYTTGTTGLPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 236 GVLLSHDNITWTAGAMSQemeINRVSGKQNTI-VSYLPLSHIAAQLTdIWIPIKIGALTFFAQPDALRGTLVYTLQEVKP 314
Cdd:cd05915 170 GVVYSHRALVLHSLAASL---VDGTALSEKDVvLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 315 TLFMGVPRIWEKMQDtikenvARSSrlRKKAFAWakmlglkvNTKRMLGKRDIPMNYRMAKALVFAKVRTSLGLDNCHAF 394
Cdd:cd05915 246 TFTAGVPTVWLALAD------YLES--TGHRLKT--------LRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 395 FSSA------SPLSQDVSEFFLSLDipigeiyGMSECSGPHTVSNKSVYRVLSCGKVLSgcknmlynqnkegvgEVCMWG 468
Cdd:cd05915 310 VVQNfvkshlESLSEEEKLTLKAKT-------GLPIPLVRLRVADEEGRPVPKDGKALG---------------EVQLKG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 469 RHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEIlITAGGENVSPIPIETLVKEKiPIISHAMLVGD 548
Cdd:cd05915 368 PWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL-IKSGGEWISSVDLENALMGH-PKVKEAAVVAI 445
|
490 500
....*....|....*....|....*
gi 569000640 549 KAKFL----CMLLTLKDRHQNLREV 569
Cdd:cd05915 446 PHPKWqerpLAVVVPRGEKPTPEEL 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-302 |
3.12e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 49 IPELFQESAERFSAYPALASKNgkkwDTLTfsqYYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAG 125
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGE----ETLD---YAELNRRAnrlAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 126 GLCVGIYATNSAEACQYVIQQANVSILIVEN--------DQQLQKILLIPPDkmetvkaivqyklplmesmanlySWNDF 197
Cdd:PRK12316 586 GAYVPLDPEYPAERLAYMLEDSGVQLLLSQShlgrklplAAGVQVLDLDRPA-----------------------AWLEG 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 198 MELGNdiPNIQLDrvilsqkANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSG-KQNTIVSYlPLSHi 276
Cdd:PRK12316 643 YSEEN--PGTELN-------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTvLQKTPFSF-DVSV- 711
|
250 260
....*....|....*....|....*.
gi 569000640 277 aaqlTDIWIPIKIGALTFFAQPDALR 302
Cdd:PRK12316 712 ----WEFFWPLMSGARLVVAAPGDHR 733
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
82-552 |
4.03e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 62.33 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 82 YYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGI---YATNSAEAcqYVIQQANvsilive 155
Cdd:PRK09192 52 YQTLRARAeagARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLplpMGFGGRES--YIAQLRG------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 ndqQLQ----KILLIPPDKMETVKAIVQyKLPLMESManlySWNDFMELgnDIPNIQLDRVilsqKANQCAVILYTSGTT 231
Cdd:PRK09192 123 ---MLAsaqpAAIITPDELLPWVNEATH-GNPLLHVL----SHAWFKAL--PEADVALPRP----TPDDIAYLQYSSGST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 232 GTPKGVLLSHDNITWTAGAMSQE-MEInrvsGKQNTIVSYLPLSHiaaqltdiwipiKIGALTFFAQPDALRGTLVYTlq 310
Cdd:PRK09192 189 RFPRGVIITHRALMANLRAISHDgLKV----RPGDRCVSWLPFYH------------DMGLVGFLLTPVATQLSVDYL-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 311 evkPTL-FMGVPRIWEKMqdtIKENVArssrlrkkAFAWAKMLGLKVNTKRMLGKRDIPMN---YR-------MAKALV- 378
Cdd:PRK09192 251 ---PTRdFARRPLQWLDL---ISRNRG--------TISYSPPFGYELCARRVNSKDLAELDlscWRvagigadMIRPDVl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 379 --FAKVRTSLGLDNcHAFFS-----------SASPLSQDVSefFLSLDIPIGEIYGMSECSGPHTVSNKSVYRvlsCGKV 445
Cdd:PRK09192 317 hqFAEAFAPAGFDD-KAFMPsyglaeatlavSFSPLGSGIV--VEEVDRDRLEYQGKAVAPGAETRRVRTFVN---CGKA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 446 LSGCKNMLYNQNKE-----GVGEVCMWGRHVFMGYLNKEEATlEALDENGWLHSGDIGRLdSHDFLYITGRIKEiLITAG 520
Cdd:PRK09192 391 LPGHEIEIRNEAGMplperVVGHICVRGPSLMSGYFRDEESQ-DVLAADGWLDTGDLGYL-LDGYLYITGRAKD-LIIIN 467
|
490 500 510
....*....|....*....|....*....|..
gi 569000640 521 GENVSPIPIETLVkEKIPIISHamlvGDKAKF 552
Cdd:PRK09192 468 GRNIWPQDIEWIA-EQEPELRS----GDAAAF 494
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
42-547 |
4.33e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 62.38 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 42 GHETPMTIPELFQESAERFSAYPALAS--KNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTAL 119
Cdd:PRK13295 19 GHWHDRTINDDLDACVASCPDKTAVTAvrLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 120 GtilagglCVGIYATnsAEACQYVIQQANVSILIVENDQqlqKILLIPP-----DKMETVKAIvQYKLPLMESM------ 188
Cdd:PRK13295 99 A-------CSRIGAV--LNPLMPIFRERELSFMLKHAES---KVLVVPKtfrgfDHAAMARRL-RPELPALRHVvvvggd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 189 -ANlySWNDFM-----ELGNDIPNIqLDRviLSQKANQCAVILYTSGTTGTPKGVLLSHdNITWTA-GAMSQEMEInrvs 261
Cdd:PRK13295 166 gAD--SFEALLitpawEQEPDAPAI-LAR--LRPGPDDVTQLIYTSGTTGEPKGVMHTA-NTLMANiVPYAERLGL---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 262 GKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFA-QPDALRgtLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSR 340
Cdd:PRK13295 236 GADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQdIWDPAR--AAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 341 LRKKAFAWAKmlglkvntkrmlgkrdIPmnyrmaKALVfAKVRTSLGLDNCHAffssasplsqdvsefflsldipigeiY 420
Cdd:PRK13295 314 LRTFLCAGAP----------------IP------GALV-ERARAALGAKIVSA--------------------------W 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 421 GMSECSGPHTVSNKSVYRVLSC--GKVLSGCKNMLYNQNKEGV-----GEVCMWGRHVFMGYLNKEEatLEALDENGWLH 493
Cdd:PRK13295 345 GMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDADGAPLpagqiGRLQVRGCSNFGGYLKRPQ--LNGTDADGWFD 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 569000640 494 SGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLVKEKiPIISHAMLVG 547
Cdd:PRK13295 423 TGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIEALLYRH-PAIAQVAIVA 474
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
95-532 |
4.42e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 62.28 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 95 KLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV-----------ENDQQLQKI 163
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVgselapkvapaVGNLRLRHV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 164 LL------IPPDKMETVKAIVQYKLPL-MESMANLYSWNDFMELGNDIPNIQLDrvilsqkANQCAVILYTSGTTGTPKG 236
Cdd:PRK08314 135 IVaqysdyLPAEPEIAVPAWLRAEPPLqALAPGGVVAWKEALAAGLAPPPHTAG-------PDDLAVLPYTSGTTGVPKG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 237 VLLSHDNITWTAGAMSqemeINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGAltffaqpdalrgTLVYtlqevkptl 316
Cdd:PRK08314 208 CMHTHRTVMANAVGSV----LWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGA------------TVVL--------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 317 fmgVPRiWEKmqdtikENVARSSRlRKKAFAWakmlglkVNTKRMLgkRDIPMNYRMAKAlVFAKVRTSLGldnchaffs 396
Cdd:PRK08314 263 ---MPR-WDR------EAAARLIE-RYRVTHW-------TNIPTMV--VDFLASPGLAER-DLSSLRYIGG--------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 397 SASPLSQDVSEFFLSL-DIPIGEIYGMSECSGPhTVSNKSVYRVLSC-----------------GKVLSgcknmlynQNK 458
Cdd:PRK08314 313 GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQ-THSNPPDRPKLQClgiptfgvdarvidpetLEELP--------PGE 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 459 egVGEVCMWGRHVFMGYLNKEEATLEA---LDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETL 532
Cdd:PRK08314 384 --VGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKR-MINASGFKVWPAEVENL 457
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
78-532 |
4.79e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 78 TFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVenD 157
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT--D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 158 QQLQKILLIPPDKMETVKAIV---------QYKLP-------LMESMANLYSWNDFMElgndipniqldrvilsqkaNQC 221
Cdd:PRK06018 119 LTFVPILEKIADKLPSVERYVvltdaahmpQTTLKnavayeeWIAEADGDFAWKTFDE-------------------NTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDN------ITWTAGAMSqemeinrvSGKQNTIVSYLPLSHIAAqltdiWipikigALTFF 295
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHRSnvlhalMANNGDALG--------TSAADTMLPVVPLFHANS-----W------GIAFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 296 A--------QPDA-LRGTLVYTLQEV-KPTLFMGVPRIWEKMQDTIKENvarssrlrkkafawakmlGLKVNTKRMLgkr 365
Cdd:PRK06018 241 ApsmgtklvMPGAkLDGASVYELLDTeKVTFTAGVPTVWLMLLQYMEKE------------------GLKLPHLKMV--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 366 dipmnyrmakalvfakvrtslgldnchAFFSSASPLSqdVSEFFLSLDIPIGEIYGMSECSGPHTVS-----------NK 434
Cdd:PRK06018 300 ---------------------------VCGGSAMPRS--MIKAFEDMGVEVRHAWGMTEMSPLGTLAalkppfsklpgDA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 435 SVYRVLSCGKVLSGCKNMLYNQNKEGV-------GEVCMWGRHVFMGYLNKEEatlEALDENGWLHSGDIGRLDSHDFLY 507
Cdd:PRK06018 351 RLDVLQKQGYPPFGVEMKITDDAGKELpwdgktfGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMR 427
|
490 500
....*....|....*....|....*
gi 569000640 508 ITGRIKEIlITAGGENVSPIPIETL 532
Cdd:PRK06018 428 ITDRSKDV-IKSGGEWISSIDLENL 451
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
369-533 |
5.90e-10 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 61.62 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 369 MNYRMAKalVFAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIP-IGEIYGMSECSGPHTVSNKS-VYRVLSCGKVL 446
Cdd:cd05929 226 MFVRLLK--LPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPiIWEYYGGTEGQGLTIINGEEwLTHPGSVGRAV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 447 SGCKNMLYNQNKE----GVGEVCMWGRHVFMgYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRiKEILITAGGE 522
Cdd:cd05929 304 LGKVHILDEDGNEvppgEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGV 381
|
170
....*....|.
gi 569000640 523 NVSPIPIETLV 533
Cdd:cd05929 382 NIYPQEIENAL 392
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
217-540 |
7.21e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 217 KANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINrvSGKQNTIVSYLPLSHiaaqltDIWIpikIGALTffa 296
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGID--LNPDDVIVSWLPLYH------DMGL---IGGLL--- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 297 QPdalrgtlvytlqevkptLFMGVPRIWEKMQDTIkenvARSSRlrkkafaWAKMLGLKVNTkrMLGKRDIPmnYRMAKA 376
Cdd:PRK05691 230 QP-----------------IFSGVPCVLMSPAYFL----ERPLR-------WLEAISEYGGT--ISGGPDFA--YRLCSE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 377 LVFAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIG-------EIYGMSECS----------GPHT--VSNKSVY 437
Cdd:PRK05691 278 RVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGfdpdsffASYGLAEATlfvsggrrgqGIPAleLDAEALA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 R----------VLSCGK------VLSGCKNMLYNQNKEGVGEVCMWGRHVFMGYLNKEEATLEA---LDENGWLHSGDIG 498
Cdd:PRK05691 358 RnraepgtgsvLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG 437
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 569000640 499 RLdSHDFLYITGRIKEILITAgGENVSPIPIETLVKEKIPII 540
Cdd:PRK05691 438 FL-RDGELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
462-532 |
7.90e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 61.60 E-value: 7.90e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000640 462 GEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITAgGENVSPIPIETL 532
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
461-547 |
9.72e-10 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 60.93 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 461 VGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKEKiPII 540
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-QINRGGEKIAAEEVENLLLAH-PAV 457
|
....*..
gi 569000640 541 SHAMLVG 547
Cdd:COG1021 458 HDAAVVA 464
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
53-252 |
1.22e-09 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 60.82 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 53 FQESAERFSAYPALASKNGkkwdTLTfsqYYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCV 129
Cdd:cd17651 1 FERQAARTPDAPALVAEGR----RLT---YAELDRRAnrlAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 130 GIYATNSAEACQYVIQQANVSilivendqqlqKILLIPPDkmetvkaivqykLPLMESMANLYSWNDFMELGNDIPNiql 209
Cdd:cd17651 74 PLDPAYPAERLAFMLADAGPV-----------LVLTHPAL------------AGELAVELVAVTLLDQPGAAAGADA--- 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000640 210 DRVILSQKANQcAVILYTSGTTGTPKGVLLSHDNIT----WTAGAMS 252
Cdd:cd17651 128 EPDPALDADDL-AYVIYTSGSTGRPKGVVMPHRSLAnlvaWQARASS 173
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
222-530 |
1.33e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.06 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQemeinRVSGKQNTIVSyLPLSHIAAqltdiwipikigaltffaqpdal 301
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHD-----RLGGPGQWLLA-LPAHHIAG----------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 rgtlvytLQEVKPTLFMGVpriwekmqDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRmlgkrdIPMnyRMAKALVFAK 381
Cdd:PRK07824 89 -------LQVLVRSVIAGS--------EPVELDVSAGFDPTALPRAVAELGGGRRYTSL------VPM--QLAKALDDPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 382 VRTSL-GLDnchAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGphtvsnKSVYRvlscGKVLSGCKNMLYNqnkeg 460
Cdd:PRK07824 146 ATAALaELD---AVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG------GCVYD----GVPLDGVRVRVED----- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 461 vGEVCMWGRHVFMGYLNKEEAtlEALDENGWLHSGDIGRLDShDFLYITGRIKEIlITAGGENVSPIPIE 530
Cdd:PRK07824 208 -GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDD-GVLTVLGRADDA-ISTGGLTVLPQVVE 272
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
88-530 |
1.35e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.48 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 88 KAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENDQQLQKILLIP 167
Cdd:PRK12406 23 RAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 168 PD----KMETVKAIVQ-YKLP--LMESMANLYSWNDFMELGNDIpniqlDRVILSQKANqcavILYTSGTTGTPKGVllS 240
Cdd:PRK12406 103 AGvtvlSVPTPPEIAAaYRISpaLLTPPAGAIDWEGWLAQQEPY-----DGPPVPQPQS----MIYTSGTTGHPKGV--R 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 241 HDNITwTAGAMSQEMEINRVSGKQNTIVSYL--PLSHIAaqltdiwiPIKIGALTFfaqpdALRGTLVytLQevkptlfm 318
Cdd:PRK12406 172 RAAPT-PEQAAAAEQMRALIYGLKPGIRALLtgPLYHSA--------PNAYGLRAG-----RLGGVLV--LQ-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 319 gvPRI-WEKMQDTIKENvarssrlrkkafawakmlglKVNTKRMlgkrdIP-MNYRMAKalVFAKVRTSLGLDNCHAFFS 396
Cdd:PRK12406 228 --PRFdPEELLQLIERH--------------------RITHMHM-----VPtMFIRLLK--LPEEVRAKYDVSSLRHVIH 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 397 SASPLSQDVSEFFLSLDIP-IGEIYGMSEcSGPHT--VSNKSVYRVLSCGKVLSGCKNMLYNQNKE-----GVGEVCMW- 467
Cdd:PRK12406 279 AAAPCPADVKRAMIEWWGPvIYEYYGSTE-SGAVTfaTSEDALSHPGTVGKAAPGAELRFVDEDGRplpqgEIGEIYSRi 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000640 468 -GRHVFMgYLNKEEAtLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIE 530
Cdd:PRK12406 358 aGNPDFT-YHNKPEK-RAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIE 418
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
222-552 |
1.71e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.51 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMsqemeINRVSGKQNTI-VSYLPLSHIAAQLTDIWIPIKIGALTFFAqpda 300
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQV-----IDALEGQEGDRgVSWLPFFHDMGLITVLLPALLGHYITFMS---- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 301 lrgtlvytlqevkPTLFMGVPRIWekmqdtIKEnVARSSRLRKKAFAWAKMLGLKVNTKRMLGKRDIPmnyrmakalvfa 380
Cdd:PRK07769 254 -------------PAAFVRRPGRW------IRE-LARKPGGTGGTFSAAPNFAFEHAAARGLPKDGEP------------ 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 381 kvrtSLGLDNCHAFFSSASPLS----QDVSEFFLSLDIP---IGEIYGMSEC-----SGPHTVSNKSVY----------- 437
Cdd:PRK07769 302 ----PLDLSNVKGLLNGSEPVSpasmRKFNEAFAPYGLPptaIKPSYGMAEAtlfvsTTPMDEEPTVIYvdrdelnagrf 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 438 -RV----------LSCGKVLSGCKNMLYNQNK-----EG-VGEVCMWGRHVFMGYLNKEEATLE---------------- 484
Cdd:PRK07769 378 vEVpadapnavaqVSAGKVGVSEWAVIVDPETaselpDGqIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlseshae 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 485 -ALDENGWLHSGDIG-RLDSHdfLYITGRIKEILITaGGENVSPIPIETLVKEKIPiishAMLVGDKAKF 552
Cdd:PRK07769 458 gAPDDALWVRTGDYGvYFDGE--LYITGRVKDLVII-DGRNHYPQDLEYTAQEATK----ALRTGYVAAF 520
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
222-543 |
2.32e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 60.36 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRvsgkQNTIVSYLPLSHiaaqltdiwipikigalTFfaqpdAL 301
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSP----EDKVFNALPVFH-----------------SF-----GL 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 RGTLVYTLQEVKPTLFMGVP---RIwekmqdtIKEnvarssrlrkkafawakmLGLKVNTKRMLGKRDIPMNY-RMAKAL 377
Cdd:PRK06814 850 TGGLVLPLLSGVKVFLYPSPlhyRI-------IPE------------------LIYDTNATILFGTDTFLNGYaRYAHPY 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 378 VFAKVRTslgldnchaFFSSASPLSQDVSEFFLS-LDIPIGEIYGMSECSgPHTVSNKSVY-RVLSCGKVLSGcknMLYN 455
Cdd:PRK06814 905 DFRSLRY---------VFAGAEKVKEETRQTWMEkFGIRILEGYGVTETA-PVIALNTPMHnKAGTVGRLLPG---IEYR 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 456 QNK-EGV---GEVCMWGRHVFMGYLNKEE-ATLEALdENGWLHSGDIGRLDSHDFLYITGRIK---EIlitaGGENVSPI 527
Cdd:PRK06814 972 LEPvPGIdegGRLFVRGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISLA 1046
|
330
....*....|....*.
gi 569000640 528 PIETLVKEKIPIISHA 543
Cdd:PRK06814 1047 AVEELAAELWPDALHA 1062
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
49-261 |
3.81e-09 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 59.09 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 49 IPELFQESAERFSAYPALASkngkkWD-TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILgFN-SVEWVVTALGTILAGG 126
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCA-----WDgSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLC-FEkSKWAVVAMLAVLKAGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 127 LCVGIYATNSAEACQYVIQQANVsilivendqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipn 206
Cdd:cd05918 75 AFVPLDPSHPLQRLQEILQDTGA--------------------------------------------------------- 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000640 207 iqldRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVS 261
Cdd:cd05918 98 ----KVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSES 148
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
211-551 |
8.97e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.18 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 211 RVILSQKANQCAVILYTSGTTGTPKGVLLSHDNItwtagaMSQEMEINRVSG--KQNTIVSYLPLSHIAAQLTDIWIPIK 288
Cdd:PRK08043 357 LAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSL------LANVEQIKTIADftPNDRFMSALPLFHSFGLTVGLFTPLL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 289 IGALTF-FAQPdalrgtLVYTLqevkptlfmgVPRIWEKMQDTIkenvarssrlrkkAFAWAKMLGlkvntkrmlgkrdi 367
Cdd:PRK08043 431 TGAEVFlYPSP------LHYRI----------VPELVYDRNCTV-------------LFGTSTFLG-------------- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 368 pmNY-RMAKALVFAKVRTSLgldnchaffSSASPLSQDVSEFFL-SLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKV 445
Cdd:PRK08043 468 --NYaRFANPYDFARLRYVV---------AGAEKLQESTKQLWQdKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 446 LSGCKNMLYN-QNKEGVGEVCMWGRHVFMGYLNKEE-ATLEA--------LDENGWLHSGDIGRLDSHDFLYITGRIKEI 515
Cdd:PRK08043 537 LPGMDARLLSvPGIEQGGRLQLKGPNIMNGYLRVEKpGVLEVptaenargEMERGWYDTGDIVRFDEQGFVQIQGRAKRF 616
|
330 340 350
....*....|....*....|....*....|....*..
gi 569000640 516 LITAgGENVSPIPIETLVKEKIPIISHAM-LVGDKAK 551
Cdd:PRK08043 617 AKIA-GEMVSLEMVEQLALGVSPDKQHATaIKSDASK 652
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-347 |
1.03e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.43 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSILIVENdqqlqkillippdkmetvkaivQYKLPLMESMANLYSWNDFMELGNDIPNIQLD 210
Cdd:PRK12316 3137 LDPEYPEERLAYMLEDSGAQLLLSQS----------------------HLRLPLAQGVQVLDLDRGDENYAEANPAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 211 rvilsqkANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLSHIAAQLTDIWIPIKIG 290
Cdd:PRK12316 3195 -------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL----GVGDRVLQFTTFSFDVFVEELFWPLMSGA 3263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 291 ALTFFAQPDALRGTLVYTLqeVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFA 347
Cdd:PRK12316 3264 RVVLAGPEDWRDPALLVEL--INSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVC 3318
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
77-547 |
1.05e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 57.83 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEN 156
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 dqQLQKIllippDKMETVKAIVQYKLPLMESMANLYSWNDfmelgnDIPN-IQLDRVILSQKA---------------NQ 220
Cdd:PRK06164 116 --GFKGI-----DFAAILAAVPPDALPPLRAIAVVDDAAD------ATPApAPGARVQLFALPdpappaaageraadpDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 221 CAVILYTSGTTGTPKGVLlsHDnitwtagamsqemeinrvsgkQNTIVSYlplSHIAAQLtdiwIPIKIGALTFFAQPda 300
Cdd:PRK06164 183 GALLFTTSGTTSGPKLVL--HR---------------------QATLLRH---ARAIARA----YGYDPGAVLLAALP-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 301 LRGtlVYTLQEVKPTLFMGVPRIWEKMQDTikenvARSSRLRKK-----AFAWAKMLglkvntKRMLGKRDIPMNYRMAK 375
Cdd:PRK06164 231 FCG--VFGFSTLLGALAGGAPLVCEPVFDA-----ARTARALRRhrvthTFGNDEML------RRILDTAGERADFPSAR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 376 ALVFAkvrtslgldnchaffsSASPLSQDVSEFFLSLDIPIGEIYGMSECSG---PHTVSNKSVYRVLSCGKVLSGCKNM 452
Cdd:PRK06164 298 LFGFA----------------SFAPALGELAALARARGVPLTGLYGSSEVQAlvaLQPATDPVSVRIEGGGRPASPEARV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 453 LYNQNKEG-------VGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLdSHD--FLYITgRIKEILiTAGGEN 523
Cdd:PRK06164 362 RARDPQDGallpdgeSGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYT-RGDgqFVYQT-RMGDSL-RLGGFL 438
|
490 500
....*....|....*....|....
gi 569000640 524 VSPIPIETLVKEkIPIISHAMLVG 547
Cdd:PRK06164 439 VNPAEIEHALEA-LPGVAAAQVVG 461
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
461-569 |
1.55e-08 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 57.34 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 461 VGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKEkIPII 540
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLLLR-HPAV 412
|
90 100 110
....*....|....*....|....*....|...
gi 569000640 541 SHAMLVGDKAKFL----CMLLTLKDRHQNLREV 569
Cdd:cd05920 413 HDAAVVAMPDELLgersCAFVVLRDPPPSAAQL 445
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-547 |
1.98e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 56.70 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 217 KANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEInrVSGKQNtIVSYLPLSHIAAQL--TDIwIPikigALTF 294
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI--RPGEVD-LATFPLFALFGPALglTSV-IP----DMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 295 FAQPDALRGTLVYTLQEVKPTLFMGVPRIWEKmqdtikenVARssrlrkkafaWAKMLGLKVNT-KRMLgkrdipmnyrM 373
Cdd:cd05910 155 TRPARADPQKLVGAIRQYGVSIVFGSPALLER--------VAR----------YCAQHGITLPSlRRVL----------S 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 374 AKALVFAKVrtslgldncHAFFSSasplsqdvsefFLSLDIPIGEIYGMSECSGPHTVSNKSVY----------RVLSCG 443
Cdd:cd05910 207 AGAPVPIAL---------AARLRK-----------MLSDEAEILTPYGATEALPVSSIGSRELLatttaatsggAGTCVG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 444 KVLSGCKNML----------YNQNKE----GVGEVCMWGRHVFMGYLNKEEAT-LEALDENG---WLHSGDIGRLDSHDF 505
Cdd:cd05910 267 RPIPGVRVRIieiddepiaeWDDTLElprgEIGEITVTGPTVTPTYVNRPVATaLAKIDDNSegfWHRMGDLGYLDDEGR 346
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 569000640 506 LYITGRIKEILITAGGENVSpIPIETlVKEKIPIISHAMLVG 547
Cdd:cd05910 347 LWFCGRKAHRVITTGGTLYT-EPVER-VFNTHPGVRRSALVG 386
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
412-533 |
2.13e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 56.54 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 412 LDIPIGEIYGMSECSG------PHTVSNKSVyrvlSCGKVLSGCKNMLYNQNkegVGEVCMWGRHVFMGYLNkeeatlEA 485
Cdd:PRK07445 253 LQLRLAPTYGMTETASqiatlkPDDFLAGNN----SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QI 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 569000640 486 LDENGWLHSGDIGRLDSHDFLYITGRIKEILITaGGENVSPIPIETLV 533
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
51-254 |
3.66e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 55.79 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASKNGKkwdtLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDES----LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSILIVEndqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqld 210
Cdd:cd12115 79 LDPAYPPERLRFILEDAQARLVLTD------------------------------------------------------- 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569000640 211 rvilsqkANQCAVILYTSGTTGTPKGVLLSHDN----ITWTAGAMSQE 254
Cdd:cd12115 104 -------PDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQWAAAAFSAE 144
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
77-261 |
5.10e-08 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 55.55 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVsiliven 156
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGA------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 dqqlqKILLIPPDKMetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkanqcAVILYTSGTTGTPKG 236
Cdd:cd17650 86 -----KLLLTQPEDL--------------------------------------------------AYVIYTSGTTGKPKG 110
|
170 180
....*....|....*....|....*
gi 569000640 237 VLLSHDNITWTAGAMSQEMEINRVS 261
Cdd:cd17650 111 VMVEHRNVAHAAHAWRREYELDSFP 135
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
75-330 |
7.04e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 54.99 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 ENDqqlqkillippdkmetvkaivqyklplmesMANLYSWN-DFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGT 233
Cdd:cd12116 91 DDA------------------------------LPDRLPAGlPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 234 PKGVLLSHDNITWTAGAMSQEMEInrvsGKQNTIVSYLPLS-HIAaqLTDIWIPIKIGALTFFAQPDALR--GTLVYTLQ 310
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRERLGL----GPGDRLLAVTTYAfDIS--LLELLLPLLAGARVVIAPRETQRdpEALARLIE 214
|
250 260
....*....|....*....|
gi 569000640 311 EVKPTLFMGVPRIWEKMQDT 330
Cdd:cd12116 215 AHSITVMQATPATWRMLLDA 234
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
39-241 |
7.32e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 39 HGPGHETPMTIPELFQESAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTA 118
Cdd:PRK05691 1123 QAPCAPAQAWLPELLNEQARQTPERIALVWDGG----SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGL 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 119 LGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVendqqlQKILLIPPDKMETVKAIVqyklplMESMaNLYSWNDfm 198
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT------QSHLLERLPQAEGVSAIA------LDSL-HLDSWPS-- 1263
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000640 199 elgnDIPNIQLDrvilsqkANQCAVILYTSGTTGTPKGVLLSH 241
Cdd:PRK05691 1264 ----QAPGLHLH-------GDNLAYVIYTSGSTGQPKGVGNTH 1295
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
459-530 |
7.39e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 55.07 E-value: 7.39e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000640 459 EGVGE-VCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILiTAGGENVSPIPIE 530
Cdd:PRK07867 350 EAIGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWM-RVDGENLGTAPIE 420
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
76-533 |
9.22e-08 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 54.80 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQ-YYEMCRkAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:cd05968 91 TLTYGElLYEVKR-LANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 EnDQQLQKILLIPP----DK----METVKAIV---QYKLPLMESMANLYSWNDFMElgndipnIQLDRVILSQKANQCAV 223
Cdd:cd05968 170 A-DGFTRRGREVNLkeeaDKacaqCPTVEKVVvvrHLGNDFTPAKGRDLSYDEEKE-------TAGDGAERTESEDPLMI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 224 IlYTSGTTGTPKGVLLSHDNITWTAGA-MSQEMEInrvsgKQNTIVSYlplshiaaqLTDI-WI--PIKI-GALTffaqp 298
Cdd:cd05968 242 I-YTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDL-----KPGDLLTW---------FTDLgWMmgPWLIfGGLI----- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 299 daLRGTLVytlqevkptLFMGVP------RIWEKMQD---TIkenvarssrlrkkafawakmLGLKVNTKRML-GKRDIP 368
Cdd:cd05968 302 --LGATMV---------LYDGAPdhpkadRLWRMVEDheiTH--------------------LGLSPTLIRALkPRGDAP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 369 MNyrmakalvfAKVRTSLgldncHAFFSSASPLSQDVSEFFLSL----DIPIGEIYGMSECSGpHTVSNKSVYRVLSCG- 443
Cdd:cd05968 351 VN---------AHDLSSL-----RVLGSTGEPWNPEPWNWLFETvgkgRNPIINYSGGTEISG-GILGNVLIKPIKPSSf 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 444 -KVLSGCKNMLYNQN----KEGVGEVCMWGRHVFM--GYLNKEEATLEAL---DENGWLHsGDIGRLDSHDFLYITGRIK 513
Cdd:cd05968 416 nGPVPGMKADVLDESgkpaRPEVGELVLLAPWPGMtrGFWRDEDRYLETYwsrFDNVWVH-GDFAYYDEEGYFYILGRSD 494
|
490 500
....*....|....*....|
gi 569000640 514 EILITAgGENVSPIPIETLV 533
Cdd:cd05968 495 DTINVA-GKRVGPAEIESVL 513
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
392-530 |
1.02e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 54.65 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 392 HAFFSSASPlsQDVSEFFLSLDIPIGEIYGMSECSG------------------------PHTVSNKSVYRVLSCGKVLS 447
Cdd:PRK13388 269 VAFGNEASP--RDIAEFSRRFGCQVEDGYGSSEGAVivvrepgtppgsigrgapgvaiynPETLTECAVARFDAHGALLN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 448 GcknmlynqnKEGVGE-VCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRiKEILITAGGENVSP 526
Cdd:PRK13388 347 A---------DEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGR-TADWMRVDGENLSA 415
|
....
gi 569000640 527 IPIE 530
Cdd:PRK13388 416 APIE 419
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
226-535 |
1.05e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 54.56 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 226 YTSGTTGTPKGVLLSHDNITwtaGAMSQEM-----EINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDA 300
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVI---ANFEQLMsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 301 lrgtlvytlqevkptlFMGVPRIWekMQdtikeNVARSSRLRKKA--FAW---------AKMLGL--------------- 354
Cdd:PRK05850 244 ----------------FLQRPARW--MQ-----LLASNPHAFSAApnFAFelavrktsdDDMAGLdlggvlgiisgserv 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 355 KVNTKRMLGKRDIPMNYRMAKalvfakVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVS-- 432
Cdd:PRK05850 301 HPATLKRFADRFAPFNLRETA------IRPSYGLAEATVYVATREPGQPPESVRFDYEKLSAGHAKRCETGGGTPLVSyg 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 433 --NKSVYRVL---SCGKVLSGcknmlynqnkeGVGEVCMWGRHVFMGYLNKEE-------ATL----EALDENGWLHSGD 496
Cdd:PRK05850 375 spRSPTVRIVdpdTCIECPAG-----------TVGEIWVHGDNVAAGYWQKPEetertfgATLvdpsPGTPEGPWLRTGD 443
|
330 340 350
....*....|....*....|....*....|....*....
gi 569000640 497 IGRLdSHDFLYITGRIKEILITAgGENVSPIPIETLVKE 535
Cdd:PRK05850 444 LGFI-SEGELFIVGRIKDLLIVD-GRNHYPDDIEATIQE 480
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
77-547 |
1.10e-07 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 54.43 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 77 LTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEn 156
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 157 dQQLQkillippDKMEtvkaivqyklplMESMAnlyswndfmelgndipniqldrvilsqkanqcaVILYTSGTTGTPKG 236
Cdd:cd05969 80 -EELY-------ERTD------------PEDPT---------------------------------LLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 237 VLLSHDnitwtagAMSQEMeinrVSGKQntivsylplsHIAAQLTDI-WIPikigaltffAQPDALRGTlVYTLqeVKPT 315
Cdd:cd05969 107 VLHVHD-------AMIFYY----FTGKY----------VLDLHPDDIyWCT---------ADPGWVTGT-VYGI--WAPW 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 316 LfMGVPriwekmqdtikeNVARSSRLrkKAFAWAKML-GLKVNTKRMlgkrdIPMNYRMAKALVFAKVRtSLGLDNCHAF 394
Cdd:cd05969 154 L-NGVT------------NVVYEGRF--DAESWYGIIeRVKVTVWYT-----APTAIRMLMKEGDELAR-KYDLSSLRFI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 395 FSSASPLSQDVSEFFLS-LDIPIGEIYGMSEcSGPHTVSNKSVYRVL--SCGKVLSGCKNMLYNQNKEGV-----GEVCM 466
Cdd:cd05969 213 HSVGEPLNPEAIRWGMEvFGVPIHDTWWQTE-TGSIMIANYPCMPIKpgSMGKPLPGVKAAVVDENGNELppgtkGILAL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 467 ---WGRhVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRIKEILITAgGENVSPIPIETLVKEKiPIISHA 543
Cdd:cd05969 292 kpgWPS-MFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEH-PAVAEA 367
|
....
gi 569000640 544 MLVG 547
Cdd:cd05969 368 GVIG 371
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
76-552 |
1.58e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 53.93 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTAlgtilAGGLCVGIYAT------NSAEACqYVIQQANV 149
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVC-----WAAERSGLYYTcvnshlTPAEAA-YIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 150 SILIVENDQqlqkiLLIPPDKMETVKAIvqyKLPLM-ESMANLYSWNDFMELGNDIPNIQLDRVILSQKanqcavILYTS 228
Cdd:PRK13391 98 RALITSAAK-----LDVARALLKQCPGV---RHRLVlDGDGELEGFVGYAEAVAGLPATPIADESLGTD------MLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 229 GTTGTPKGVL--LSHDNItwtAGAMSQEMEINRVSGKQNTIVsYL---PLSHiAAQLTDIWIPIKIGALTF----FAQPD 299
Cdd:PRK13391 164 GTTGRPKGIKrpLPEQPP---DTPLPLTAFLQRLWGFRSDMV-YLspaPLYH-SAPQRAVMLVIRLGGTVIvmehFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 300 ALRGTLVY--TLQEVKPTLFMgvpriwekmqdtikenvarssrlrkkafawakmlglkvntkRMLgkrDIPmnyrmakal 377
Cdd:PRK13391 239 YLALIEEYgvTHTQLVPTMFS-----------------------------------------RML---KLP--------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 378 vfAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIP-IGEIYGMSECSGPHTV-SNKSVYRVLSCGKVLSGCKNMLYN 455
Cdd:PRK13391 266 --EEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFGDLHILDD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 456 QNKE---GV-GEVCMWGRHVFMgYLNKEEATLEALDENG-WLHSGDIGRLDSHDFLYITGRiKEILITAGGENVSPIPIE 530
Cdd:PRK13391 344 DGAElppGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAE 421
|
490 500
....*....|....*....|..
gi 569000640 531 TLvkekipIISHAMlVGDKAKF 552
Cdd:PRK13391 422 NL------LITHPK-VADAAVF 436
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
222-530 |
1.87e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 53.86 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVllshdnitwtagamSQEMEINRVSGKQNTIVSylplshIAAQLTDIwipiKIGALTFFAQPdal 301
Cdd:PRK13390 151 AVMLYSSGTTGFPKGI--------------QPDLPGRDVDAPGDPIVA------IARAFYDI----SESDIYYSSAP--- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 302 rgtlvytlqevkptLFMGVPRIWEKMQDTIKENVARSSRlrkkaFAWAKMLGlKVNTKRMLGKRDIP-MNYRMAKalVFA 380
Cdd:PRK13390 204 --------------IYHAAPLRWCSMVHALGGTVVLAKR-----FDAQATLG-HVERYRITVTQMVPtMFVRLLK--LDA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 381 KVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPI-------GEIYGMSECSGPHTVSNKSvyrvlSCGKVLSGCKNML 453
Cdd:PRK13390 262 DVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIvyeyyssTEAHGMTFIDSPDWLAHPG-----SVGRSVLGDLHIC 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 454 YNQNKE----GVGEVCMWGRHVFMGYLNKEEATLEALDENG--WLHSGDIGRLDSHDFLYITGRiKEILITAGGENVSPI 527
Cdd:PRK13390 337 DDDGNElpagRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQ 415
|
...
gi 569000640 528 PIE 530
Cdd:PRK13390 416 ETE 418
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
48-261 |
3.49e-07 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 52.82 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKNGKkwdtLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQ----LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGIYATNSAEACQYVIQQANVSILIVENDqqlqkillippdkmetvkaivqyklplmesmaNLyswndfmelgndipni 207
Cdd:cd17644 77 YVPLDPNYPQERLTYILEDAQISVLLTQPE--------------------------------NL---------------- 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 208 qldrvilsqkanqcAVILYTSGTTGTPKGVLLSHD---NITWTAGAMSQEMEINRVS 261
Cdd:cd17644 109 --------------AYVIYTSGSTGKPKGVMIEHQslvNLSHGLIKEYGITSSDRVL 151
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
222-532 |
4.38e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 52.60 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 222 AVILYTSGTTGTPKGVL--LSHDNITWTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAqltdiwipikigaLTFFAQPD 299
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAP-------------LRFGMSAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 300 ALRGTLVYTlqevkptlfmgvpriwEKmqdtikenvarssrlrkkaFAWAKMLGL----KVNTKRMlgkrdIP-MNYRMA 374
Cdd:PRK08276 210 ALGGTVVVM----------------EK-------------------FDAEEALALieryRVTHSQL-----VPtMFVRML 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 375 KalVFAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPI-GEIYGMSECSGPhTVSNK--------SVYR-VLSCGK 444
Cdd:PRK08276 250 K--LPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIiHEYYASSEGGGV-TVITSedwlahpgSVGKaVLGEVR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 445 VLSGcknmlyNQNKEGVGEVCMwgrhVFM-------GYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRiKEILI 517
Cdd:PRK08276 327 ILDE------DGNELPPGEIGT----VYFemdgypfEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMI 395
|
330
....*....|....*
gi 569000640 518 TAGGENVSPIPIETL 532
Cdd:PRK08276 396 ISGGVNIYPQEIENL 410
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-241 |
5.80e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.04 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 82 YYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENDq 158
Cdd:PRK12316 2031 YAELDSRAnrlAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH- 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 159 qlqkillippdkmetvkaiVQYKLPLMESMANLY-----SWNDFMElgnDIPNIQLDrvilsqkANQCAVILYTSGTTGT 233
Cdd:PRK12316 2110 -------------------LLERLPLPAGVARLPldrdaEWADYPD---TAPAVQLA-------GENLAYVIYTSGSTGL 2160
|
....*...
gi 569000640 234 PKGVLLSH 241
Cdd:PRK12316 2161 PKGVAVSH 2168
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-547 |
6.15e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 51.61 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 224 ILYTSGTTGTPKGVLLSHDNITWTAGAmsqemeiNRVSGKQNTIVSYLpLSHIAAqltdiwipiKIGALTFFAQPDALRG 303
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMG-------GADFGTGEFTPSED-AHKAAA---------AAAGTVMFPAPPLMHG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 304 TLVYTLQevkpTLFMGVPRIwekmqdtikenVARSSRLRKKAfAWAKMLGLKVNTKRMLGkrDIpmnyrMAKALVFAKVR 383
Cdd:cd05924 71 TGSWTAF----GGLLGGQTV-----------VLPDDRFDPEE-VWRTIEKHKVTSMTIVG--DA-----MARPLIDALRD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 384 ------TSLgldncHAFFSSASPLSQDVSEFFLSL--DIPIGEIYGMSECSGPHTVSNKSvyRVLSCGK---------VL 446
Cdd:cd05924 128 agpydlSSL-----FAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFTGSGHSAG--SGPETGPftranpdtvVL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 447 SGCKNMLynqnKEGVGEVCMWGR--HVFMGYLNKEEATLEALDE-NG--WLHSGDIGRLDSHDFLYITGRiKEILITAGG 521
Cdd:cd05924 201 DDDGRVV----PPGSGGVGWIARrgHIPLGYYGDEAKTAETFPEvDGvrYAVPGDRATVEADGTVTLLGR-GSVCINTGG 275
|
330 340
....*....|....*....|....*.
gi 569000640 522 ENVSPIPIETLVKeKIPIISHAMLVG 547
Cdd:cd05924 276 EKVFPEEVEEALK-SHPAVYDVLVVG 300
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
65-242 |
1.39e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 51.05 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 65 ALASKNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVI 144
Cdd:PRK04319 62 ALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 145 QQANVSILIVeNDQQLQKIlliPPDKMETVKAIVQYKLPlMESMANLYSWNDFMELGNDIPNIQ-LDRvilsqkaNQCAV 223
Cdd:PRK04319 142 EDSEAKVLIT-TPALLERK---PADDLPSLKHVLLVGED-VEEGPGTLDFNALMEQASDEFDIEwTDR-------EDGAI 209
|
170
....*....|....*....
gi 569000640 224 ILYTSGTTGTPKGVLLSHD 242
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHN 228
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
75-245 |
1.79e-06 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 50.38 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 ENDQQlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkanqcAVILYTSGTTGTP 234
Cdd:cd17643 91 DPDDL--------------------------------------------------------------AYVIYTSGSTGRP 108
|
170
....*....|.
gi 569000640 235 KGVLLSHDNIT 245
Cdd:cd17643 109 KGVVVSHANVL 119
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
47-568 |
1.98e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.53 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 47 MTIPELFQESAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGG 126
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRPGLIDELG----TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 127 LCVGIYATNSAEACQYVIQQANVSILIVenDQQLqkILLIPPDKMETVKAIvqyklplmesmaNLYSWNDfmelgndIPN 206
Cdd:PRK13382 119 DILLLNTSFAGPALAEVVTREGVDTVIY--DEEF--SATVDRALADCPQAT------------RIVAWTD-------EDH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 207 IQLDRVILSQKANQ--------CAVILYTSGTTGTPKGVLLSHDNitwTAGAMSqemeinrvsgkqnTIVSYLPLSH--- 275
Cdd:PRK13382 176 DLTVEVLIAAHAGQrpeptgrkGRVILLTSGTTGTPKGARRSGPG---GIGTLK-------------AILDRTPWRAeep 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 276 --IAAQLTDIWipiKIGALTFFAqpdALRGTLVY--------TLQEV---KPTLFMGVPRIWEKMQDTIKENVARSSrlr 342
Cdd:PRK13382 240 tvIVAPMFHAW---GFSQLVLAA---SLACTIVTrrrfdpeaTLDLIdrhRATGLAVVPVMFDRIMDLPAEVRNRYS--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 343 kkafawakmlglkvntkrmlgkrdipmnyrmAKALVFAKvrtslgldnchaffSSASPLSQD-VSEFFLSLDIPIGEIYG 421
Cdd:PRK13382 311 -------------------------------GRSLRFAA--------------ASGSRMRPDvVIAFMDQFGDVIYNNYN 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 422 MSECSGPHTVSNKSVYRVL-SCGKVLSGCKNMLYNQNKEGV--GEV-CMWGRH--VFMGYLNKeeATLEALDenGWLHSG 495
Cdd:PRK13382 346 ATEAGMIATATPADLRAAPdTAGRPAEGTEIRILDQDFREVptGEVgTIFVRNdtQFDGYTSG--STKDFHD--GFMASG 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000640 496 DIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKeKIPIISHAMLVG-DKAKF---LCMLLTLKDRHQNLRE 568
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVEKTLA-THPDVAEAAVIGvDDEQYgqrLAAFVVLKPGASATPE 496
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-244 |
2.20e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 50.93 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 31 EVLLRLSKHGPGHETPMTIPELF-QESAERFSAypaLASKNGKKwdTLTfsqYYEMCRKA---AKSLIKLGLQRFQCVGI 106
Cdd:PRK12467 1558 QILEGWNATHTGYPLARLVHQLIeDQAAATPEA---VALVFGEQ--ELT---YGELNRRAnrlAHRLIALGVGPEVLVGI 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 107 LGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEndqqlqkillippdkmetvkAIVQYKLPLME 186
Cdd:PRK12467 1630 AVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ--------------------SHLQARLPLPD 1689
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000640 187 SMANLyswndFMELGNDIPNIQLD-RVILSQKANQCAVILYTSGTTGTPKGVLLSHDNI 244
Cdd:PRK12467 1690 GLRSL-----VLDQEDDWLEGYSDsNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL 1743
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
211-245 |
2.53e-06 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 50.06 E-value: 2.53e-06
10 20 30
....*....|....*....|....*....|....*
gi 569000640 211 RVILSQKANQCAVILYTSGTTGTPKGVLLSHDNIT 245
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLA 120
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
51-244 |
3.05e-06 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 49.86 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALASkNGKKWdtlTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVG 130
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD-RGQSL---TYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 131 IYATNSAEACQYVIQQANVSILIVENDqqlqkillippdkmetvkaivqyklplmesmaNLyswndfmelgndipniqld 210
Cdd:cd17645 78 IDPDYPGERIAYMLADSSAKILLTNPD--------------------------------DL------------------- 106
|
170 180 190
....*....|....*....|....*....|....
gi 569000640 211 rvilsqkanqcAVILYTSGTTGTPKGVLLSHDNI 244
Cdd:cd17645 107 -----------AYVIYTSGSTGLPKGVMIEHHNL 129
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-257 |
3.62e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 51 ELFQESAERFSAYPALaskngkKWDTLTFSqYYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:PRK12316 4555 QLVAERARMTPDAVAV------VFDEEKLT-YAELNRRAnrlAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGA 4627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGIYATNSAEACQYVIQQANVSILIVENDQQLQkillippdkmetvkaivqykLPLMESMANLY-----SWNDFMElgN 202
Cdd:PRK12316 4628 YVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR--------------------LPIPDGLASLAldrdeDWEGFPA--H 4685
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000640 203 DiPNIQLDrvilsqkANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEI 257
Cdd:PRK12316 4686 D-PAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYEL 4732
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
218-543 |
4.36e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 49.62 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 218 ANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQE--MEINRVSGKqnTIVSYLPLSHIAAQLtdiWI--PIKIGALT 293
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglNWVTWVVGE--TTYSPLPATHIGGLW---WIltCLMHGGLC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 294 FFAQPDALRGTLVYTLQEVKPTLFmgVPRIWEKMQDTIKENVARSSRLRKKAFAwakmlglkvntkrmlGKRDIPMNYRM 373
Cdd:PRK05857 243 VTGGENTTSLLEILTTNAVATTCL--VPTLLSKLVSELKSANATVPSLRLVGYG---------------GSRAIAADVRF 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 374 AKAlvfAKVRTSlgldnchaffssasplsqdvsefflsldipigEIYGMSE--CSG---PhtVSNKSVYRVL--SCGKVL 446
Cdd:PRK05857 306 IEA---TGVRTA--------------------------------QVYGLSEtgCTAlclP--TDDGSIVKIEagAVGRPY 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 447 SGCKNMLYNQN-----KEGVGEVCMWGR------HVFMGYLNKEEATLEALDEnGWLHSGDIGRLDSHDFLYITGRIKEI 515
Cdd:PRK05857 349 PGVDVYLAATDgigptAPGAGPSASFGTlwikspANMLGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEM 427
|
330 340
....*....|....*....|....*...
gi 569000640 516 LITaGGENVSPIPIETlVKEKIPIISHA 543
Cdd:PRK05857 428 IIC-GGVNIAPDEVDR-IAEGVSGVREA 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-244 |
6.76e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:PRK05691 2189 TLHGLFAAQAARTPQAPALTFAG----QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGIYATNSAEACQYVIQQANVSILIveNDQQLQKILLIPPDKMEtvkaivqyKLPLMESMANLYSWNDfmelgNDIPNI 207
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLL--SDRALFEALGELPAGVA--------RWCLEDDAAALAAYSD-----APLPFL 2329
|
170 180 190
....*....|....*....|....*....|....*..
gi 569000640 208 QLDRvilsqkaNQcAVILYTSGTTGTPKGVLLSHDNI 244
Cdd:PRK05691 2330 SLPQ-------HQ-AYLIYTSGSTGKPKGVVVSHGEI 2358
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
76-278 |
8.00e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 48.50 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NdqqlqkillippdkmetvkaivqyklplmesmanlyswndfmelgndipniqldrvilsqkanqcAVILYTSGTTGTPK 235
Cdd:cd05940 83 A-----------------------------------------------------------------ALYIYTSGTTGLPK 97
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000640 236 GVLLSHDNItWTAGAMSQEMEINrvsGKQNTIVSYLPLSHIAA 278
Cdd:cd05940 98 AAIISHRRA-WRGGAFFAGSGGA---LPSDVLYTCLPLYHSTA 136
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
441-540 |
1.12e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.20 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 441 SCGKVLSGCKNMLYNQNKE------GVGEVCMWGRHVFMGYLNKEEATLE------------------ALDENGWLHSGD 496
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGaelpdgEVGEIWLHGDNIGRGYWGRPEETERtfgaklqsrlaegshadgAADDGTWLRTGD 482
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 569000640 497 IG-RLDSHdfLYITGRIKEiLITAGGENVSPIPIETLVKEKIPII 540
Cdd:PRK12476 483 LGvYLDGE--LYITGRIAD-LIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
457-531 |
1.29e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.84 E-value: 1.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000640 457 NKEGVGEVCMWGRHVFMGYLNKEeatleALDENGWLHSGDIGRLdSHDFLYITGRIKEiLITAGGENVSPIPIET 531
Cdd:PRK05851 368 AGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYL-VDGGLVVCGRAKE-LITVAGRNIFPTEIER 435
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
64-250 |
1.53e-05 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 47.63 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 64 PALASKNgkkwDTLTfsqYYEMCRKA---AKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEAC 140
Cdd:cd17652 4 PAVVFGD----ETLT---YAELNARAnrlARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 141 QYVIQQANVSILIVENDqqlqkillippdkmetvkaivqyklplmesmaNLyswndfmelgndipniqldrvilsqkanq 220
Cdd:cd17652 77 AYMLADARPALLLTTPD--------------------------------NL----------------------------- 95
|
170 180 190
....*....|....*....|....*....|
gi 569000640 221 cAVILYTSGTTGTPKGVLLSHDNITWTAGA 250
Cdd:cd17652 96 -AYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
50-244 |
1.55e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 47.66 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 50 PELFQESAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCV 129
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGR----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 130 GIYATNSAEACQYVIQQANVSILIVENDQQLQkilliPPDkmETVKAIVQYKLPLMEsmanlyswndfmelgndiPNIQL 209
Cdd:cd17646 77 PLDPGYPADRLAYMLADAGPAVVLTTADLAAR-----LPA--GGDVALLGDEALAAP------------------PATPP 131
|
170 180 190
....*....|....*....|....*....|....*
gi 569000640 210 DRVILSQKAnqcAVILYTSGTTGTPKGVLLSHDNI 244
Cdd:cd17646 132 LVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
48-244 |
4.24e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 46.42 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 48 TIPELFQESAERFSAYPALASKNgkkwDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGL 127
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGD----RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 128 CVGIYATNSAEACQYVIQQANVSILIVEnDQQLQKILLIPPDkMETVKAIVQYklplmesmanlyswNDfmELGNDIPN- 206
Cdd:PRK07798 80 PVNVNYRYVEDELRYLLDDSDAVALVYE-REFAPRVAEVLPR-LPKLRTLVVV--------------ED--GSGNDLLPg 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000640 207 -IQLDRVILSQKANQCAV--------ILYTSGTTGTPKGVLLSHDNI 244
Cdd:PRK07798 142 aVDYEDALAAGSPERDFGerspddlyLLYTGGTTGMPKGVMWRQEDI 188
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
223-547 |
4.51e-05 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 45.76 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 223 VILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNTivsyLPLSHIaaqltdiwipikigaltffaqpdalr 302
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNS----GPLFHI-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 303 GTLVYTLqevkPTLFMG-----VPRiwekmqdTIKENVAR---SSRLRKkAFAWAKMLG--LKVNTKrmlGKRDipmnyr 372
Cdd:cd17636 54 GTLMFTL----ATFHAGgtnvfVRR-------VDAEEVLElieAERCTH-AFLLPPTIDqiVELNAD---GLYD------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 373 makalvfakvrtslgLDNCHAFFSS---ASPLSQDVSEFFLSldiPIGeiYGMSECSGPHTVSNKSVYRVLSCGKVLSGC 449
Cdd:cd17636 113 ---------------LSSLRSSPAApewNDMATVDTSPWGRK---PGG--YGQTEVMGLATFAALGGGAIGGAGRPSPLV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 450 K-NMLYNQNKE----GVGEVCMWGRHVFMGYLNKEEATLEALdENGWLHSGDIGRLDSHDFLYITGRiKEILITAGGENV 524
Cdd:cd17636 173 QvRILDEDGREvpdgEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENI 250
|
330 340
....*....|....*....|...
gi 569000640 525 SPIPIETLVKEkIPIISHAMLVG 547
Cdd:cd17636 251 YPAEVERCLRQ-HPAVADAAVIG 272
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
222-243 |
5.98e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 45.66 E-value: 5.98e-05
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
368-547 |
6.56e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 45.59 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 368 PMNYRM---AKALVFAKVRTSLgldncHAFFSSASPLSQDVSEFF-LSLDIPIGEIYGMSECSGPhtVSN----KSVYRV 439
Cdd:cd05973 186 PTAYRLlmaAGAEVPARPKGRL-----RRVSSAGEPLTPEVIRWFdAALGVPIHDHYGQTELGMV--LANhhalEHPVHA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 440 LSCGKVLSGCKNMLYNQNKEGVGE-------------VCMWgrhvFMGYLNKEEATLEAldenGWLHSGDIGRLDSHDFL 506
Cdd:cd05973 259 GSAGRAMPGWRVAVLDDDGDELGPgepgrlaidiansPLMW----FRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSF 330
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569000640 507 YITGRIKEILITAgGENVSPIPIETLVKEKiPIISHAMLVG 547
Cdd:cd05973 331 SFIGRADDVITMS-GYRIGPFDVESALIEH-PAVAEAAVIG 369
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
75-243 |
7.43e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 ENDQQLQkILLIPPDKMETVKAIVQYKLPlmesmanlYSWNDFMElGNDIpniqldrvilsqkanqcAVILYTSGTTGTP 234
Cdd:PRK04813 106 TEELPLE-ILGIPVITLDELKDIFATGNP--------YDFDHAVK-GDDN-----------------YYIIFTSGTTGKP 158
|
....*....
gi 569000640 235 KGVLLSHDN 243
Cdd:PRK04813 159 KGVQISHDN 167
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
461-530 |
8.16e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 45.27 E-value: 8.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000640 461 VGEVCMWGRHVFMGYLNKEEATLEA--LDENG--WLHSGDIGRLDSHDFLYITGRIKEILITAGGeNVSPIPIE 530
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGG-TLYTIPCE 459
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
468-546 |
9.80e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 44.98 E-value: 9.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000640 468 GRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEiLITAGGENVSPIPIETLVKeKIPIISHAMLV 546
Cdd:PRK10946 387 GPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-QINRGGEKIAAEEIENLLL-RHPAVIHAALV 463
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
33-530 |
1.71e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 33 LLR-LSKHGPGHETPMTIpelfqeSAERFSAYPALASKNGkkwdTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNS 111
Cdd:PRK13383 26 LLReASRGGTNPYTLLAV------TAARWPGRTAIIDDDG----ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 112 VEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVEND--QQL----QKILLIPPdkmETVKAivqyklplM 185
Cdd:PRK13383 96 RGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEfaERIagadDAVAVIDP---ATAGA--------E 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 186 ESMANlyswndfmelgndiPNIqldrvilsqkANQCAVILYTSGTTGTPKGVLLShDNITWTAGAMSQEMEINRV-SGKQ 264
Cdd:PRK13383 165 ESGGR--------------PAV----------AAPGRIVLLTSGTTGKPKGVPRA-PQLRSAVGVWVTILDRTRLrTGSR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 265 NTIVsyLPLSHiaaqltdiwipikigALTFfaqpdalrGTLVYTLQevkptlfMGVPRIWEKMQDTiKENVARSSRLRKK 344
Cdd:PRK13383 220 ISVA--MPMFH---------------GLGL--------GMLMLTIA-------LGGTVLTHRHFDA-EAALAQASLHRAD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 345 AFAwakmlGLKVNTKRMLgkrDIPMNYRMAKALVFAKVRTSLG--LDNCHA--FFSSASPLsqdVSEFFLSLDIPIGEIY 420
Cdd:PRK13383 267 AFT-----AVPVVLARIL---ELPPRVRARNPLPQLRVVMSSGdrLDPTLGqrFMDTYGDI---LYNGYGSTEVGIGALA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 421 GMSEC-SGPHTVsnksvyrvlscGKVLSGCKNMLYNQNKEGVGEVCMwGRHVFMGYLNKEEAT----LEALDenGWLHSG 495
Cdd:PRK13383 336 TPADLrDAPETV-----------GKPVAGCPVRILDRNNRPVGPRVT-GRIFVGGELAGTRYTdgggKAVVD--GMTSTG 401
|
490 500 510
....*....|....*....|....*....|....*
gi 569000640 496 DIGRLDSHDFLYITGRiKEILITAGGENVSPIPIE 530
Cdd:PRK13383 402 DMGYLDNAGRLFIVGR-EDDMIISGGENVYPRAVE 435
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
224-249 |
5.25e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.82 E-value: 5.25e-04
10 20
....*....|....*....|....*.
gi 569000640 224 ILYTSGTTGTPKGVLlsHDnitwTAG 249
Cdd:PRK00174 250 ILYTSGSTGKPKGVL--HT----TGG 269
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
76-251 |
6.54e-04 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 42.62 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVE 155
Cdd:TIGR02188 88 KITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 156 NDQ-------QLQKI----LLIPPDKMETVkaIVqyklplmesmanlyswndFMELGNDIPNIQLDR------VILSQKA 218
Cdd:TIGR02188 168 DEGlrggkviPLKAIvdeaLEKCPVSVEHV--LV------------------VRRTGNPVVPWVEGRdvwwhdLMAKASA 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000640 219 nQCAV----------ILYTSGTTGTPKGVLlsHDnitwTAGAM 251
Cdd:TIGR02188 228 -YCEPepmdsedplfILYTSGSTGKPKGVL--HT----TGGYL 263
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
75-291 |
1.26e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.51 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 75 DTLTFSQYYEMCRKAAKSLIK-LGLQRFQCVGILGFNSVEWVVTALGtiLAG-GLCVGIYATNS-AEACQYVIQQANVSI 151
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLG--LAKlGCPVAFLNTNIrSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 152 LIVENDQQ--LQKILliPPDKMETVKaiVQYKLPLMESmANLYSWNDFMELGNDIPNIQLDRVILSQKANqcAVILYTSG 229
Cdd:cd05938 82 LVVAPELQeaVEEVL--PALRADGVS--VWYLSHTSNT-EGVISLLDKVDAASDEPVPASLRAHVTIKSP--ALYIYTSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000640 230 TTGTPKGVLLSHDNItWTAGAMSqemeinRVSGKQNTIVSY--LPLSHIAAQLTDIWIPIKIGA 291
Cdd:cd05938 155 TTGLPKAARISHLRV-LQCSGFL------SLCGVTADDVIYitLPLYHSSGFLLGIGGCIELGA 211
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
220-244 |
1.32e-03 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 41.23 E-value: 1.32e-03
10 20
....*....|....*....|....*
gi 569000640 220 QCAVILYTSGTTGTPKGVLLSHDNI 244
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSV 119
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
224-251 |
1.38e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 41.39 E-value: 1.38e-03
10 20
....*....|....*....|....*...
gi 569000640 224 ILYTSGTTGTPKGVLlsHDnitwTAGAM 251
Cdd:cd05966 236 ILYTSGSTGKPKGVV--HT----TGGYL 257
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
76-327 |
2.86e-03 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 40.15 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 76 TLTFSQYYEMCRKAAKSLIKLGLQRF-QCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIV 154
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 155 EndqqlqkillippDKMETVkaivqyklplmesmanlyswndfmelgNDIpniqldrvilsqkanqcAVILYTSGTTGTP 234
Cdd:cd05958 90 A-------------HALTAS---------------------------DDI-----------------CILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000640 235 KGVLLSHDNITWTAGAMSQEmeinrVSGKQ--NTIVSYLPLSHIAAQLTDIWIPIKIGAlTFFAQPDALRGTLVYTLQEV 312
Cdd:cd05958 113 KATMHFHRDPLASADRYAVN-----VLRLRedDRFVGSPPLAFTFGLGGVLLFPFGVGA-SGVLLEEATPDLLLSAIARY 186
|
250
....*....|....*
gi 569000640 313 KPTLFMGVPRIWEKM 327
Cdd:cd05958 187 KPTVLFTAPTAYRAM 201
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
218-237 |
3.06e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 40.32 E-value: 3.06e-03
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
224-238 |
8.13e-03 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 39.22 E-value: 8.13e-03
|
| |
